Relevant bibliographies by topics / Proteine lmg

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  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Proteine lmg'

Author: Grafiati
Published: 4 June 2021
Last updated: 17 February 2022

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Journal articles on the topic "Proteine lmg"

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Kuczak, Michał, and Ewa Kurczyńska. "Cell Wall Composition as a Marker of the Reprogramming of the Cell Fate on the Example of a Daucus carota (L.) Hypocotyl in Which Somatic Embryogenesis Was Induced." International Journal of Molecular Sciences 21, no. 21 (October 30, 2020): 8126. http://dx.doi.org/10.3390/ijms21218126.

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Changes in the composition of the cell walls are postulated to accompany changes in the cell’s fate. We check whether there is a relationship between the presence of selected pectic, arabinogalactan proteins (AGPs), and extensins epitopes and changes in cell reprogramming in order to answer the question of whether they can be markers accompanying changes of cell fate. Selected antibodies were used for spatio-temporal immunolocalization of wall components during the induction of somatic embryogenesis. Based on the obtained results, it can be concluded that (1) the LM6 (pectic), LM2 (AGPs) epitopes are positive markers, but the LM5, LM19 (pectic), JIM8, JIM13 (AGPs) epitopes are negative markers of cells reprogramming to the meristematic/pluripotent state; (2) the LM8 (pectic), JIM8, JIM13, LM2 (AGPs) and JIM11 (extensin) epitopes are positive markers, but LM6 (pectic) epitope is negative marker of cells undergoing detachment; (3) JIM4 (AGPs) is a positive marker, but LM5 (pectic), JIM8, JIM13, LM2 (AGPs) are negative markers for pericycle cells on the xylem pole; (4) LM19, LM20 (pectic), JIM13, LM2 (AGPs) are constitutive wall components, but LM6, LM8 (pectic), JIM4, JIM8, JIM16 (AGPs), JIM11, JIM12 and JIM20 (extensins) are not constitutive wall components; (5) the extensins do not contribute to the cell reprogramming.
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Larsen, Nadja, Mette Boye, Henrik Siegumfeldt, and Mogens Jakobsen. "Differential Expression of Proteins and Genes in the Lag Phase of Lactococcus lactis subsp. lactis Grown in Synthetic Medium and Reconstituted Skim Milk." Applied and Environmental Microbiology 72, no. 2 (February 2006): 1173–79. http://dx.doi.org/10.1128/aem.72.2.1173-1179.2006.

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ABSTRACT We investigated protein and gene expression in the lag phase of Lactococcus lactis subsp. lactis CNRZ 157 and compared it to the exponential and stationary phases. By means of two-dimensional polyacrylamide gel electrophoresis, 28 highly expressed lag-phase proteins, implicated in nucleotide metabolism, glycolysis, stress response, translation, transcription, cell division, amino acid metabolism, and coenzyme synthesis, were identified. Among the identified proteins, >2-fold induction and down-regulation in the lag phase were determined for 12 proteins in respect to the exponential phase and for 18 proteins in respect to the stationary phase. Transcriptional changes of the lag-phase proteins in L. lactis were studied by oligonucleotide microarrays. Good correlation between protein and gene expression studies was demonstrated for several differentially expressed proteins, including nucleotide biosynthetic enzymes, adenylosuccinate synthase (PurA), IMP dehydrogenase (GuaB), and aspartate carbamoyl transferase (PyrB); heat-shock protein DnaK; serine hydroxymethyl transferase (GlyA); carbon catabolite control protein (CcpA); elongation factor G (FusA); and cell division protein (FtsZ).
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Coenye, Tom, Elke Vanlaere, Enevold Falsen, and Peter Vandamme. "Stenotrophomonas africana Drancourt et al. 1997 is a later synonym of Stenotrophomonas maltophilia (Hugh 1981) Palleroni and Bradbury 1993." International Journal of Systematic and Evolutionary Microbiology 54, no. 4 (July 1, 2004): 1235–37. http://dx.doi.org/10.1099/ijs.0.63093-0.

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Type and reference strains of Stenotrophomonas maltophilia and Stenotrophomonas africana were compared with each other and with the type strains of other Stenotrophomonas species, using SDS-PAGE of whole-cell proteins, DNA–DNA hybridization and extensive biochemical characterization. S. maltophilia LMG 958T and S. africana LMG 22072T had very similar whole-cell-protein patterns and were also biochemically very similar. A DNA–DNA binding level of 70 % between both type strains confirmed that S. africana and S. maltophilia represent the same taxon. It is concluded that S. africana is a later synonym of S. maltophilia.
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El-Behaedi, Salma, Rebekah Landsman, Michael Rudloff, Emily Kolyvas, Rakan Albalawy, Xianyu Zhang, Tapan Bera, Keith Collins, Serguei Kozlov, and Christine Alewine. "Protein Synthesis Inhibition Activity of Mesothelin Targeting Immunotoxin LMB-100 Decreases Concentrations of Oncogenic Signaling Molecules and Secreted Growth Factors." Toxins 10, no. 11 (October 31, 2018): 447. http://dx.doi.org/10.3390/toxins10110447.

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LMB-100 is a mesothelin-targeted recombinant immunotoxin (iTox) that carries a modified Pseuodomonas exotoxin A (PE) payload. PE kills cells by inhibiting synthesis of new proteins. We found that treatment of pancreatic cancer cells with LMB-100 for 24–48 h did not change total protein level despite inducing protein synthesis inhibition (PSI). Further, increased levels of ubiquitinated proteins were detected, indicating that cells may have limited ability to compensate for PSI by reducing protein degradation. Together, these data suggest that PE depletes concentrations of a minority of cellular proteins. We used reverse phase protein array and Luminex assay to characterize this subset. LMB-100 decreased the abundance of 24 of 32 cancer-related proteins (including Bcl-x, Her2, Her3 and MUC16) without compensatory increases in other analytes. Further, cancer cells failed to maintain extracellular concentrations of cancer cell secreted growth factors (CCSGFs), including Vascular Endothelial Growth Factor (VEGF) following treatment with cytostatic LMB-100 doses both in culture and in mouse tumors. Decreased VEGF concentration did not change tumor vasculature density, however, LMB-100 caused tissue-specific changes in concentrations of secreted factors made by non-cancer cells. In summary, our data indicate that PSI caused by cytostatic LMB-100 doses preferentially depletes short-lived proteins such as oncogenic signaling molecules and CCSGFs.
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Kuniyoshi, Hisato, Kotaro Baba, Ryu Ueda, Shunzo Kondo, Wakae Awano, Naoto Juni, and Daisuke Yamamoto. "lingerer, a Drosophila Gene Involved in Initiation and Termination of Copulation, Encodes a Set of Novel Cytoplasmic Proteins." Genetics 162, no. 4 (December 1, 2002): 1775–89. http://dx.doi.org/10.1093/genetics/162.4.1775.

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Abstract In an effort to uncover genetic components underlying the courtship behavior of Drosophila melanogaster, we have characterized a novel gene, lingerer (lig), mutations of which result in abnormal copulation. Males carrying a hypomorphic mutation in lig fail to withdraw their genitalia upon termination of copulation, but display no overt abnormalities in their genitalia. A severe reduction in the dosage of the lig gene causes repeated attempted copulations but no successful copulations. Complete loss of lig function results in lethality during early pupal stages. lig is localized to polytene segment 44A on the second chromosome and encodes three alternatively spliced transcripts that generate two types of 150-kD proteins, Lig-A and Lig-B, differing only at the C terminus. Lig proteins show no similarity to known proteins. However, a set of homologous proteins in mammals suggest that Drosophila Lig belongs to a family of proteins that share five highly conserved domains. Lig is a cytoplasmic protein expressed in the central nervous system (CNS), imaginal discs, and gonads. Lig-A expression is selectively reduced in lig mutants and the ubiquitous supply of this protein at the beginning of metamorphosis restores the copulatory defects of the lig mutant. We propose that lig may act in the nervous system to mediate the control of copulatory organs during courtship.
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Nilsen, Trine, Ingolf F. Nes, and Helge Holo. "Enterolysin A, a Cell Wall-Degrading Bacteriocin from Enterococcus faecalis LMG 2333." Applied and Environmental Microbiology 69, no. 5 (May 2003): 2975–84. http://dx.doi.org/10.1128/aem.69.5.2975-2984.2003.

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ABSTRACT A novel antimicrobial protein, designated enterolysin A, was purified from an Enterococcus faecalis LMG 2333 culture. Enterolysin A inhibits growth of selected enterococci, pediococci, lactococci, and lactobacilli. Antimicrobial activity was initially detected only on solid media, but by growing the bacteria in a fermentor under optimized production conditions (MRS broth with 4% [wt/vol] glucose, pH 6.5, and a temperature between 25 and 35°C), the bacteriocin activity was increased to 5,120 bacteriocin units ml−1. Enterolysin A production was regulated by pH, and activity was first detected in the transition between the logarithmic and stationary growth phases. Killing of sensitive bacteria by enterolysin A showed a dose-response behavior, and the bacteriocin has a bacteriolytic mode of action. Enterolysin A was purified, and the primary structure was determined by combined amino acid and DNA sequencing. This bacteriocin is translated as a 343-amino-acid preprotein with an sec-dependent signal peptide of 27 amino acids, which is followed by a sequence corresponding to the N-terminal part of the purified protein. Mature enterolysin A consists of 316 amino acids and has a calculated molecular weight of 34,501, and the theoretical pI is 9.24. The N terminus of enterolysin A is homologous to the catalytic domains of different cell wall-degrading proteins with modular structures. These include lysostaphin, ALE-1, zoocin A, and LytM, which are all endopeptidases belonging to the M37 protease family. The N-terminal part of enterolysin A is linked by a threonine-proline-rich region to a putative C-terminal recognition domain, which shows significant sequence identity to two bacteriophage lysins.
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Bagon, Bernadette B., Ju Kyoung Oh, Valerie Diane V. Valeriano, Edward Alain B. Pajarillo, and Dae-Kyung Kang. "Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis." Molecules 26, no. 18 (September 20, 2021): 5695. http://dx.doi.org/10.3390/molecules26185695.

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Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics. Specifically, proteomics has helped determine and describe the physiological changes that lactic acid bacteria undergo in specific conditions, especially in the host gut. In particular, the extracellular proteome, or exoproteome, of lactobacilli contains proteins specific to host– or environment–microbe interactions. Using gel-free, label-free ultra-high performance liquid chromatography tandem mass spectrometry, we explored the exoproteome of the probiotic candidate Lactobacillus mucosae LM1 subjected to bile treatment, to determine the proteins it may use against bile stress in the gut. Bile stress increased the size of the LM1 exoproteome, secreting ribosomal proteins (50S ribosomal protein L27 and L16) and metabolic proteins (lactate dehydrogenase, phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate dehydrogenases, among others) that might have moonlighting functions in the LM1 bile stress response. Interestingly, membrane-associated proteins (transporters, peptidase, ligase and cell division protein ftsH) were among the key proteins whose secretion were induced by the LM1 bile stress response. These specific proteins from LM1 exoproteome will be useful in observing the proposed bile response mechanisms via in vitro experiments. Our data also reveal the possible beneficial effects of LM1 to the host gut.
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Faye, Therese, Dag Anders Brede, Thor Langsrud, Ingolf F. Nes, and Helge Holo. "An Antimicrobial Peptide Is Produced by Extracellular Processing of a Protein from Propionibacterium jensenii." Journal of Bacteriology 184, no. 13 (July 1, 2002): 3649–56. http://dx.doi.org/10.1128/jb.184.13.3649-3656.2002.

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ABSTRACT A protease-activated antimicrobial peptide (PAMP) and its inactive precursor were purified from the culture supernatant of Propionibacterium jensenii LMG 3032 and characterized at the molecular level. PAMP is a 64-amino-acid cationic peptide of 6,383 Da with physicochemical features similar to those of bacteriocins from gram-positive bacteria. This peptide displayed bactericidal activity against several propionibacteria and lactobacilli. DNA sequencing indicated that the PAMP-encoding gene (pamA) is translated as a proprotein of 198 amino acids with an N-terminal signal peptide of 27 amino acids and that PAMP constitutes the C-terminal part of this precursor. The amino acid sequence of pro-PAMP showed no similarity to those of other known proteins. By using activity tests and mass spectrometry, we showed that PAMP was formed upon protease treatment of the precursor protein. The propionibacteria produced the PAMP precursor constitutively during growth up to a level of ∼4 mg/liter, but the producing bacteria were unable to activate the precursor. The requirement for an external protease represents a novel strategy for generating antimicrobial peptides.
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Popielarska-Konieczna, Marzena, Katarzyna Sala, Mohib Abdullah, Monika Tuleja, and Ewa Kurczyńska. "Extracellular matrix and wall composition are diverse in the organogenic and non-organogenic calli of Actinidia arguta." Plant Cell Reports 39, no. 6 (March 30, 2020): 779–98. http://dx.doi.org/10.1007/s00299-020-02530-2.

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Abstract Key message Differences in the composition and the structural organisation of the extracellular matrix correlate with the morphogenic competence of the callus tissue that originated from the isolated endosperm of kiwifruit. Abstract The chemical composition and structural organisation of the extracellular matrix, including the cell wall and the layer on its surface, may correspond with the morphogenic competence of a tissue. In the presented study, this relationship was found in the callus tissue that had been differentiated from the isolated endosperm of the kiwiberry, Actinidia arguta. The experimental system was based on callus samples of exactly the same age that had originated from an isolated endosperm but were cultured under controlled conditions promoting either an organogenic or a non-organogenic pathway. The analyses which were performed using bright field, fluorescence and scanning electron microscopy techniques showed significant differences between the two types of calli. The organogenic tissue was compact and the outer walls of the peripheral cells were covered with granular structures. The non-organogenic tissue was composed of loosely attached cells, which were connected via a net-like structure. The extracellular matrices from both the non- and organogenic tissues were abundant in pectic homogalacturonan and extensins (LM19, LM20, JIM11, JIM12 and JIM20 epitopes), but the epitopes that are characteristic for rhamnogalacturonan I (LM5 and LM6), hemicellulose (LM25) and the arabinogalactan protein (LM2) were detected only in the non-organogenic callus. Moreover, we report the epitopes, which presence is characteristic for the Actinidia endosperm (LM21 and LM25, heteromannan and xyloglucan) and for the endosperm-derived cells that undergo dedifferentiation (loss of LM21 and LM25; appearance or increase in the content of LM5, LM6, LM19, JIM11, JIM12, JIM20, JIM8 and JIM16 epitopes).
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Louis, Magali, Jacques R. Poortmans, Marc Francaux, Jacques Berré, Nathalie Boisseau, Eric Brassine, Daniel J. R. Cuthbertson, et al. "No effect of creatine supplementation on human myofibrillar and sarcoplasmic protein synthesis after resistance exercise." American Journal of Physiology-Endocrinology and Metabolism 285, no. 5 (November 2003): E1089—E1094. http://dx.doi.org/10.1152/ajpendo.00195.2003.

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Muscle hypertrophy during resistance training is reportedly increased by creatine supplementation. Having previously failed to find an anabolic effect on muscle protein turnover at rest, either fed or fasted, we have now examined the possibility of a stimulatory effect of creatine in conjunction with acute resistance exercise. Seven healthy men (body mass index, 23 ± 2 kg/m2, 21 ± 1 yr, means ± SE) performed 20 × 10 repetitions of leg extension-flexion at 75% one-repetition maximum in one leg, on two occasions, 4 wk apart, before and after ingesting 21 g/day creatine for 5 days. The subjects ate ∼21 g maltodextrin + 6 g protein/h for 3 h postexercise. We measured incorporation of [1-13C]leucine into quadriceps muscle proteins in the rested and exercised legs. Leg protein breakdown (as dilution of [2H5]phenylalanine) was also assessed in the exercised and rested leg postexercise. Creatine supplementation increased muscle total creatine by ∼21% ( P < 0.01). Exercise increased the synthetic rates of myofibrillar and sarcoplasmic proteins by two- to threefold ( P < 0.05), and leg phenylalanine balance became more positive, but creatine was without any anabolic effect.
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Dissertations / Theses on the topic "Proteine lmg"

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Durand, Jean-Pierre. "Contribution a l'etude du groupe des proteines nucleaires de faible mobilite electrophoretique (lmg)." Nantes, 1988. http://www.theses.fr/1988NANT2010.

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Zheng, Qiaoyun. "Study of Cancer Related Proteins: LRG-1 and PD-L1." Cleveland State University / OhioLINK, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=csu1495735827467521.

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Lam, Ching-po. "Analysis of LMP-1 variants in EBV related Hodgkin's disease." Click to view the E-thesis via HKUTO, 2003. http://sunzi.lib.hku.hk/hkuto/record/B3197109X.

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Smith, Ewan James. "Identification and characterisation of anti-angiogenic protein fragments in venous leg ulcer fluid." Thesis, University of Hertfordshire, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.409458.

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Gannon, Benedict William. "Specific lgG antibody responses to the surface layer proteins of Campylobacter fetus subsp. fetus." Thesis, University of Bristol, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.424043.

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Dickinson, Jared M. "A method to study in vivo protein synthesis in slow and fast twitch muscle fibers and initial measurements in humans." Muncie, Ind. : Ball State University, 2009. http://cardinalscholar.bsu.edu/773.

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林正甫 and Ching-po Lam. "Analysis of LMP-1 variants in EBV related Hodgkin's disease." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 2003. http://hub.hku.hk/bib/B3197109X.

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Murello, Anna. "La spettroscopia di forza basata sull'AFM nello studio dello spazio conformazionale e dei processi aggregativi di proteine prioniche." Master's thesis, Alma Mater Studiorum - Università di Bologna, 2015. http://amslaurea.unibo.it/8878/.

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Le malattie neurodegenerative sono caratterizzate da aggregazione proteica, dipendente dalla perdita della usuale struttura fisiologica funzionale delle proteine coinvolte, a favore di conformazioni tossiche (patologiche). Il modello corrente descrive questi cambiamenti conformazionali come eventi rari e ritiene che non esista una sola conformazione patogena, ma che tali possibili conformazioni siano piuttosto eterogenee. La caratterizzazione di queste strutture è, di conseguenza, difficile con le tradizionali tecniche in bulk che permettono di studiare solo la conformazione media e non rendono possibile il riconoscimento delle caratteristiche dei conformeri individuali. Lo sviluppo delle tecniche di singola molecola ha permesso di studiare in modo approfondito le conformazioni possibili. In questo lavoro la spettroscopia di forza di singola molecola basata sull'AFM viene applicata a PrP (proteina responsabile delle encefalopatie spongiformi trasmissibili). Si studiano gli equilibri conformazionali del monomero e quelli di costrutti oligomerici, allo scopo di caratterizzare gli step iniziali dei processi aggregativi. Nel corso di questo lavoro di tesi è stato, in particolare, sviluppato un sistema di analisi dati, al fine di studiare in modo quantitativo le distribuzioni di eventi ottenute. Grazie a tale strumento è stato possibile riconoscere i segnali di unfolding della conformazione nativa del monomero e notare come essa sia presente anche in costrutti oligomerici, ad indicare come questo ripiegamento sia stabile anche in presenza di più monomeri ravvicinati. Si è osservato l'effetto del pH sulla stabilità di tale struttura, notando come pH acidi destabilizzino il ripiegamento nativo. Inoltre si è studiato il ruolo dell'orientazione dei monomeri nella formazione di strutture dimeriche. Monomeri e oligomeri di PrP sono stati descritti come proteine parzialmente strutturate il cui panorama energetico contiene molti minimi locali, dando origine a parecchie conformazioni transienti.
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Chaligné, Ronan. "Signalisation par le récepteur de la thrombopoïétine et syndromes myéloprolifératifs non-LMC." Paris 11, 2009. http://www.theses.fr/2009PA11T053.

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Moulin, Pauline. "Caractérisation du transporteur de zinc Adc/Lmb de Streptococcus agalactiae." Thesis, Tours, 2017. http://www.theses.fr/2017TOUR3308/document.

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Dans cette étude, le transporteur ABC de zinc de Streptococcus agalactiae, première cause d’infections materno-foetale en France, a été caractérisé. Nous avons montré que ce transporteur se compose, du complexe perméase-ATPase AdcCB, associé à trois protéines membranaires Lmb, AdcA et AdcAII redondantes dans la fixation de zinc. Ce transporteur comporte également deux protéines Sht et ShtII, retrouvées au niveau de la paroi, et nécessaires aux protéines Lmb et AdcAII pour la capture de zinc. L’absence d’un transporteur fonctionnel, par la triple délétion des gènes lmb, adcA et adcAII ou du complexe adcCB, a révélé une inhibition de la croissance et une perturbation de la division de la bactérie lorsqu’elle se trouve dans un environnement carencé en zinc. De plus, nous avons montré que ce transporteur de zinc participe à la survie de la bactérie en milieux biologiques humains, comme le liquide amniotique ou le LCR, où la bactérie est retrouvée lors d’infections, suggérant l’importance du transporteur lors du processus infectieux. Ces résultats ont mis en évidence, pour la première fois, que le zinc assure des fonctions biologiques vitales pour S. agalactiae et que, dans des conditions de forte carence en zinc, le transporteur Adc/Lmb représente le principal système d’acquisition de zinc de la bactérie
In this study, the zinc-ABC transporter of Streptococcus agalactiae, the first cause of materno-foetal infections in France, was characterized. We showed that this transporter is composed of an AdcCB permease-ATPase complex in association with three membrane-associated proteins Lmb, AdcA and AdcAII, which are redundant in zinc-binding. This transporter also possesses two proteins Sht and ShtII, which are associated to the cell wall, and that are necessary for the Lmb and AdcAII proteins for zinc capture. The absence of a functional transporter, by the triple deletion of the lmb, adcA and adcAII genes or the adcCB complex, revealed a growth inhibition and a disruption of the division of the bacterium when it is in a zinc-restricted environment. Furthermore, we showed that the zinc-ABC transporter contributes to the survival of the bacterium in human biological fluids, as the amniotic fluid or the cerebrospinal fluid, where the bacterium is found during infections, suggesting the importance of the transporter during the infectious process. These results hightlighted, for the first time, that zinc has biologically vital functions in S. agalactiae and that, under high zinc deficiency conditions, the Adc/Lmb transporter is the main zinc acquisition system of the bacterium
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Books on the topic "Proteine lmg"

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Meurig Thomas, John. Architects of Structural Biology. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780198854500.001.0001.

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Designed for the non-specialist, the explanations and illustrations used here describe the work, personalities, collaborations, and idiosyncrasies of four of the most distinguished Nobel Laureates of the twentieth century. They exploited a discovery made over a century ago about the nature of X-rays, and thereby created a new branch of science. This enabled them to elucidate, in atomic detail, the structure and mode of action of molecules of the living world: enzymes, vitamins, and viruses, as well as antibiotics. Perutz and Kendrew, from their pioneering work using X-ray diffraction on haemoglobin and myoglobin, the proteins that transport and store oxygen in all animals, led them to establish in 1962 one of the most successful research centres ever—the Laboratory of Molecular Biology (LMB) in Cambridge. Medicines discovered there are used worldwide to treat leukaemia, arthritis, and other diseases. Their work also led to the creation in the United States of the Protein Data Bank that guides scientists in understanding the misfolding of proteins, which cause Alzheimer’s disease, Parkinson’s disease, and other neurodegenerative diseases. This book is first a memoir of these scientists and their contemporaries, many of them friends of the author. Second, it is an insight into the great excitement associated with structural molecular biology, which directly informs our understanding of ourselves. Third, it describes how two renowned research centres in the United Kingdom—the LMB and the Davy-Faraday Research Laboratory—achieved iconic status. It also highlights the importance of the popularization of science, of which Bragg, Perutz, and Kendrew, as well as Dorothy Hodgkin (who solved the structures of penicillin and vitamin B12) were experts.
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Kavanagh, David Christopher. Extracellular alkaline protease production by Pseudomonas aeruginosa in venous leg ulcers. 1996.

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Wang, David Derwoei. The role of Epstein-Barr virus latent infection membrane protein (LMP) in cell transformation. 1988.

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Waired. Diabetic Food Journal: A Daily Log for Tracking Calories, Carbs, Sugars, Fiber, Protein, Fat ... in Your Day. Independently Published, 2020.

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Pill, Jason. Diabetes Log Book: Vegetarian Vegan Protein Sweet Animal Lover Gift 120 Pages, 59 Weeks, 6X9 Inches, Blood Sugar and Hypertension Journal. Independently Published, 2020.

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Journal, Blank Notebook. Notebook: Vegan Workout Gift Powered Plants Protein Vegetarian Blank Notebook Journal with College Rule Lined Pages Marble Size Work Out Log 8. 5inx11in for Men and Women. Independently Published, 2020.

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Book chapters on the topic "Proteine lmg"

1

Woolf, Thomas B., and Michael Tychko. "The third leg: Molecular dynamics simulations of lipid binding proteins." In Lipid Binding Proteins within Molecular and Cellular Biochemistry, 143–56. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4929-1_17.

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Finkelstein, Alexey V., Nikita V. Dovidchenko, Olga M. Selivanova, Maria Yu Suvorina, Alexey K. Surin, and Oxana V. Galzitskaya. "Determination of the Size of the Primary and Secondary Folding Nuclei of Protofibrils from the Concentration Dependence of the Rate and the Lag-Time of Their Formation." In Physical Biology of Proteins and Peptides, 47–66. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-21687-4_3.

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Hatzubai, A., M. Anafi, G. Klein, and D. Sulitzeanu. "Expression of the EBV-Encoded Membrane Protein (LMP) in Virally Transformed Cells." In Epstein-Barr Virus and Human Disease, 255–56. Totowa, NJ: Humana Press, 1987. http://dx.doi.org/10.1007/978-1-4612-4590-2_56.

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Giraldo, Patricia, Magdalena Ruiz, M. Itria Ibba, Craig F. Morris, Maryke T. Labuschagne, and Gilberto Igrejas. "Durum Wheat Storage Protein Composition and the Role of LMW-GS in Quality." In Wheat Quality For Improving Processing And Human Health, 73–108. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-34163-3_5.

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Boos, Harald, Rudolf Berger, Cornelia Kuklik-Roos, and Nikolaus Mueller-Lantzsch. "Epstein-Barr Virus Protein (LMP) Expression is Enhanced by Serum, TPA or Butyrate." In Epstein-Barr Virus and Human Disease, 229–33. Totowa, NJ: Humana Press, 1987. http://dx.doi.org/10.1007/978-1-4612-4590-2_49.

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Branen, J. K., M. Kwon, and N. J. Engeseth. "Expression of Antisense Acyl Carrier Protein-4 (LMI-ACP) Reduces Lipid Content in Arabidopsis Leaf Tissue." In Advanced Research on Plant Lipids, 73–76. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-017-0159-4_16.

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Fu, Bin, and Wei Wang. "A $2^{O(n^{1-{1\over d}}\log n)}$ Time Algorithm for d-Dimensional Protein Folding in the HP-Model." In Automata, Languages and Programming, 630–44. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-540-27836-8_54.

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Mohammed Ali Jassim, Marwa, Majid Mohammed Mahmood, and Murtada Hafedh Hussein. "Human Herpetic Viruses and Immune Profiles." In Innate Immunity in Health and Disease. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96340.

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Herpesviruses are large, spherical, enveloped viral particles with linear double-stranded DNA genome. Herpesvirus virion consists of an icosahedral capsid containing viral DNA, surrounded by a protein layer called tegument, and enclosed by an envelope consisting of a lipid bilayer with various glycoproteins. Herpesviruses persist lifelong in their hosts after primary infection by establishing a latent infection interrupted recurrently by reactivations. The Herpesviridae family is divided into three subfamilies; α-herpesviruses, β-herpesviruses, and γ-herpesviruses based on the genome organization, sequence homology, and biological properties. There are eight human herpes viruses: Herpes simplex virus type 1 and 2 (HSV-1, −2) andVaricella-zoster virus (VZV), which belong to the α-herpesvirus subfamily; Human cytomegalovirus (HCMV), and Human herpesvirus type 6 and 7 (HHV-6,HHV-7), which belong to the β-herpesvirus subfamily; and Epstein–Barr virus (EBV) and Kaposi’s sarcoma-associated herpesvirus (KSHV) or Human herpesvirus 8 (HHV-8), which belong to the γ-herpesvirus subfamily. Within this chapter, we summarize the current knowledge about EBV and CMV, regarding their genome organization, structural characteristics, mehanisms of latency, types of infections, mechanisms of immune escape and prevention. Epstein–Barr Virus (EBV) genome encodes over 100 proteins, of which only (30) proteins are well characterized, including the proteins expressed during latent infection and lytic cycle proteins. Based on major variation in the EBNA-2 gene sequence, two types of EBV are recognized, EBV type 1 and 2. Epstein–Barr virus types occur worldwide and differ in their geographic distribution depending on the type of virus. EBV spreads most commonly through bodily fluids, especially saliva. However, EBV can also spread through blood, blood transfusions, and organ transplantations. The EBV is associated with many malignant diseases such as lymphomas, carcinomas, and also more benign such as infectious mononucleosis, chronic active infection. The EBV has also been suggested as a trigger/cofactor for some autoimmune diseases. Overall, 1–1.5% of the cancer burden worldwide is estimated to be attributable to EBV The latently infected human cancer cells express the most powerful monogenic proteins, LMP-1 and LMP-2(Latent Membrane Protein-1,-2), as well as Epstein–Barr Nuclear Antigens (EBNA) and two small RNAs called Epstein–Barr Encoded Small RNAs (EBERs). The EBV can evade the immune system by its gene products that interfering with both innate and adaptive immunity, these include EBV-encoded proteins as well as small noncoding RNAs with immune-evasive properties. Currently no vaccine is available, although there are few candidates under evaluation. Human cytomegalovirus (HCMV) is a ubiquitous beta herpesvirus type 5 with seroprevalence ranges between 60 to 100% in developing countries. CMV is spread from one person to another, usually by direct and prolonged contact with bodily fluids, mainly saliva, but it can be transmitted by genital secretions, blood transfusion and organ transplantation. In addition, CMV can be transmitted vertically from mother to child. CMV infection can result in severe disease for babies, people who receive solid organ transplants or bone marrow/stem cell transplants and people with severe immune suppression such as advanced human immunodeficiency virus (HIV) infection. The HCMV has several mechanisms of immune system evasion. It interferes with the initiation of adaptive immune responses, as well as prevent CD8+ and CD4+ T cell recognition interfering with the normal cellular MHC Class I and MHC Class II processing and presentation pathways. Challenges in developing a vaccine include adeptness of CMV in evading the immune system. Though several vaccine candidates are under investigation.
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"Sarcomeric Proteins in LGM D." In Molecular Mechanisms of Muscular Dystrophies, 153–59. CRC Press, 2006. http://dx.doi.org/10.1201/9781498713962-16.

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"Protein-based lms and coatings." In Edible Coatings and Films to Improve Food Quality, 26–91. CRC Press, 2011. http://dx.doi.org/10.1201/b11082-6.

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Conference papers on the topic "Proteine lmg"

1

Kalyan, N. K., S. G. Lee, W.-T. Hum, R. Hartzell, M. Levner, and P. P. Hung. "IN VITRO STUDIES ON THE BINDING OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (t-PA) AND UROKINASE (u-PA) TO LIVER MEMBRANES." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643603.

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The plasminogen activators, t-PA and u-PA, are glycoproteins known to be involved in homeostasis of the blood clotting system, and thus are of potential clinical use in the treatment of thrombosis. Several in vivo studies have shown that both t-PA and u-PA are quickly removed from the blood circulation, predominantly by the liver. The mechanism by which the liver removes these proteins is not understood. To delineate this, we conducted in vitro studies of binding of PAs or their derivatives to isolated mouse liver membranes utilizing a functional assay developed in our laboratory. The assay consisted of initial binding of t-PA to liver membranes followed by centrifugation to pellet the membranes and the assay of the activity of the membrane-bound t-PA by a fibrin-agar plate method. The bound t-PA, which retained complete enzymic activity, could be dissociated by SDS treatment in an undegraded form as shown by SDS-PAGE. The binding of t-PA as well as u-PA was very fast and did not compete with glycoproteins or sugars containing the terminal galactose, mannose and N-acetylglucosamine residues. Furthermore, the treatment of t-PA with neuraminidase and/or periodate oxidation did not affect its binding characteristics. These data suggest that the carbohydrate moieties of t-PA and u-PA, unlike many glycoproteins, do not mediate their binding to the liver. This raised the possibility of the liver binding sequence being located in the protein backbone, especially the non-protease domains which are known to determine the biological specificities of PAs. The relative binding of u-PA and its low molecular weight (LMW) derivative containing only the protease domain, to the liver membranes was studied. Unlike u-PA and t-PA, LMW-urokinase did not bind significantly. This suggests that the protein sequence containing the non-protease domains, rather than the carbohydrate moieties of PAs contain the information necessary for binding to the liver and possibly their clearance from the blood circulation.
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Schleuning, W. D. "THE BIOCHEMISTRY AND CELL BIOLOGY OF SINGLE CHAIN UROKINASE TYPE PLASMINOGEN ACTIVATOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642956.

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Urokinase was discovered in the late nineteenth century, as an enzymatic principle in urine, that initiates the dissolution of blood clots. The basis of this phenomenon was recognized more than fifty years ago as the activation of plasminogen, the precursor of a tryptic protease, then known as profibrinolysin. Despite this long history, detailed data on the biochemistry of plasminogen activation have only become available recently. Urokinase (now designated urokinase-type plasminogen activator : u-PA) is synthesized and secreted as a single chain polypeptide (Mr-: 53,000) by many cell types. Single chain u-PA (scu-PA) is with equal justification called prourokinase (pro-u-PA), notwithstanding its low catalytic activity for synthetic peptide substrates and plasminogen, as most proenzymes of proteases display a certain degree of activity. The structure of pro-u-PA has been elucidated by protein and cDNA sequencing. It consists of three domains, exhibiting characteristic homology to other proteins: a serine protease domain, homologous to trypsin, chymotrypsin and elastase; a kringle domain, likewise found in prothrombin, plasminogen, tissue-type plasminogen activator (t-PA) and Factor XII; and an epidermal growth factor (EGF)-like domain, found in many other proteins, including certain clotting factors. Pro-u-PA is activated by the cleavage of its LYS158-Ile159 h1 bY either plasmin or kallikrein. This cleavage leads to a high increase of Kcat values with respect to both plasminogen and synthetic peptide substrates, but apparently to a reduction of its affinity to plasminogen. Thrartoin inactivates pro-u-PA irreversibly by the cleavage of the Arg156-Phe157 bond. U-PA but not pro-u-PA rapidly forms ccnplexes with plasminogen activator inhibitors (PAI)-l and PAI-2: second order rate constants Kass are respectively > 107 and 0.9xl06 (M-11sec-1). Unknown enzymes process pro-u-PA and u-PA to low molecular weight (LMW) pro-u-PA and LMW u-PA (Mr: 33,000) by cutting off a fragment consisting of the kr ingle and the EGF—like region. Pro—u—PA mediated plasminogen activation is fibrin dependent in vivo, and to a certain degree in vitro. Hie biochemical basis of this fibrin specificity is at present uncertain, although there are reports indicating that it may require polyvalent cations. Through its EGF-like region HMW pro-u-PA and HMW u-PA are capable of binding to specific membrane protein receptors which are found on many cells. Thus, u-PA activity may be restricted to the cell surface. According to a recent report, binding of u—PA to the receptor may also mediate signal transduction in auto- or paracrine growth control. In cells permissive for the respective pathways, pro-u-PA gene transcription is stimulated by mechanisms of signal transduction, that include the cAMP, the tyrosine specific kinase and the protein kinase C dependent pathways. Glucocorticoid hormones downregulate pro-u-PA gene transcription in cells where the gene is canstitutively expressed. Although different cells vary greatly in their response to agents that stimulate urokinase biosynthesis, growth factors and other mitogens are in many cases effective inducers. Significantly elevated levels of u-PA are also found in many malignant tissues. These findings and many others suggest that plasminogen activation by u-PA provides localized extracellular matrix degradation which is required for invasive growth, cell migration and other forms of tissue remodelling. Fibrin represents in this view only a variant of an extracellular matrix, which is provided through the clotting system in the case of an emergency.
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Morrien-Salomons, M. M., A. Sturk, M. V. Huisman, J. Borm, H. R. Büller, and J. W. ten Cate. "EVALUATION OF COMMERCIAL PROTEIN C ASSAYS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644314.

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Plasma protein C inactivates the activated coagulation factors V and VIII. The assay of protein C is important, because a protein C deficiency is associated with a thrombotic tendency. We therefore evaluated 5 commercial assays in 49 normal volunteers, 48 patients suspected of deep vein thrombosis (DVT) of the leg but with negative impedance plethysmography (IPG), and 52 patients with DVT proven by IPG. The assays were rocket electrophoresis (Merz and Dade antibody), ELISA (Boehringer Mannheim), 2 chromogenic activity assays (Behringwerke and Kabi) and a clotting assay (Behringwerke). Coumarin therapy was used by 13 DVT positive, and 3 DVT negative patients. Results are presented in the table.TABLE: In correlation 1 and 2, the assay results all non-coumarin treated individuals (n = 133) were compared with rocket electrophoresis and ELISA resp.In the non-coumarin treated patients, both in the DVT positive and in the DVT negative patient group one protein C deficiency was detected by all assays.Based upon the large assay VC (ROCKET) and normal range (B. CLOT), and poor correlation of the assays with the ELISA (ROCKET, B. CLOT) we conclude that the ELISA, B.CHROM and K.CHROM are to be preferred. However, as B.CHROM does not need a plasma absorption step it is somewhat preferable for activity assays.
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Schick, B. P., C. J. Walsh, and T. Jenkins-West. "PROTEOGLYCANS AND SULFATED PROTEINS OF PLATELETS: CHARACTERIZATION AND RESPONSE TO THROMBIN AND ADP." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643642.

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The proteoglycans (PG) and sulfated proteins of guinea pig platelets were labeled in vivo by intraperitoneal injection of (35S)sulfate. At 3 days after injection, platelets contained 3 distinct populations of chondroitin-6-sulfate proteoglycans which together constitute about 65% of the cellular (35S) label. Most PG elute from a DEAE-Sephacel column with 4M Gdn HC1 (PG-1, 87%), and elute at Kav 0.12 on Sepharose CL-6B. The PG-1 can be resolved by SDS-PAGE into two fractions. The remainder (PG-2, 13%) elutes from the DEAE-Sephacel column with 4M Gdn HCl/2% Triton X-100 or 2% CHAPS, and has a Kav of 0.07 on Sepharose CL-6B. About 20-25% of the cell (35S) label elutes from DEAE-Sephacel in the wash-through or with 0.23M NaCl, and can be resolved by SDS-PAGE into at least 8 distinct bands which we have tentatively characterized as sulfated glycoproteins. The remainder of the (35S) is in low molecular weight (LMW) material which does not adhere to DEAE-Sephacel and has not been further characterized.Platelets were treated with either thrombin or ADP, and the cells were then separated from the supernatant by centrifugation. The radiolabeled molecules in the supernatant and the cells were analyzed by DEAE-Sephacel and Sepharose CL-6B column chromatography. About 65% of the total cell (35S) was released from the cells by thrombin. Most of this radiolabel adhered to the DEAE-Sephacel column, and was found to be PG-1. The remainder of the released (35S) was about half the LMW material. In contrast, only 10-15% of the (35S)labeled material retained by the cells adhered to DEAE-Sephacel and was found to be PG-2. The remainder of the (35S)-labeled material retained by the platelets was the sulfated proteins and the LMW material. ADP caused release of about 15% of the (35S), and this was found to be in part PG-1 and in part the LMW material, but not PG-2. None of the (35S)-labeled molecules appeared to be degraded during platelet activation. We suggest that the PG-1 represent the a-granule and PG-2 the membrane proteoglycans. The sulfated proteins have not been described previously. Their role is not known, but we hypothesize that they may form part of the negative charge of the glycocalix and thus be part of the reactive surface of the platelet.
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Dautzenberg, M. D., F. Monge, A. M. Fischer, R. Girot, and P. Cornu. "COAGULATION AND FIBRINOLYSIS IN SICKLE CELL DISEASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643056.

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Sickled erythocytes appear to be primarily responsible for occlusion of microvasculature in patients with homozygous sickle cell disease (SCD), but it is unknown whether the activation of the coagulation pathway is also contributory to these vaso-occlusive crisis and other complications as leg ulcers, aseptic necrosis of bone, strokes. Thus, we studied coagulation and fibrinolysis parameters in 12 patients (ages 2 to 26 years with SCD, in steady-state, far from thrombotic events which occurred in 3 of them) to determine if it would be possible to detect a high-risk group for thrombosis. We were surprised to observe that all the vitamin K dependent factors levels (II, VII+X, IX, protein C) were found next to the lowest values of the normal range.But in 3 out of 12 patients, protein C was significantly lower and 2 of them have had thrombotic events (stroke, leg ulcers). Factor V level was in the normal range except for 3 patients with low levels. As other authors, we observed normal fibrinogen, plasminogen and a 2 antiplasmin values and always very high factor VIII levels. Antithrombin III activity was normal or even high contrasting with the lower levels of the other factors synthesized in the liver. However all these abnormalities seem to balance since the thrombin generation test performed in the patients plasmas are in the normal range. As a marker of high-risk group for thrombosis, fibrin-D-Dimer levels (using a latex bead agglutination assay) were measured and found to be positive in 4 patients, 3 of them having suffered from thrombosis associated in two cases with a protein C deficiency. Thus, if the hemostatic modifications observed are involved in the mechanism of thrombosis, fibrin-D-Dimer and protein C seem to be the most significant parameters in this study.
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El-Behaedi, Salma, Rebekah Landsman, Michael Rudloff, Emily Kolyvas, Rakan AlBalawy, and Christine Alewine. "Abstract 3964: Mesothelin targeting immunotoxin LMB-100 alters the profile of tumor-secreted proteins." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3964.

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Kakkar, S., E. Melissari, and V. V. Kakkar. "CONGENITAL SEVERE PROTEIN C DEFICIENCY IN ADULTS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644304.

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We (Melissari et al, 1985, T.R. 29 [1985] 641) were the first to identify the occurrence of severe protein C deficiency in an adult with thrombophilia and undetectable protein C levels. This report documents our clinical and laboratory resuts of this patient and his family, as well as another 8 patients, in two more, unrelated families. In these unique families with members suffering from severe protein C deficiency (≤6%), no one had experienced neonatal purpura fulminans. Symptoms started mainly in their early twenties, except in 2 patients who first had symptoms at the ages of 11 and 13. The expression of the protein C deficiency was mainly recurrent superficial and deep iliofemoral vein thrombosis and pulmonary embolism. The protein C deficiency was also expressed as generalised peritonitis due to massive messenteric vein thrombosis, cavernus sinus, renal vein thrombosis and priapism. In one of these families, five members died of intra-abdominal thrombosis before the age of 40. A compensated diffuse intra- vascular coagulation syndrome was observed during massive thromboembolic attacks as evidenced by high levels of D-Dimer (≥5000ng/ml). The treatment of choice was heparin or urokinase (with the exception of one patient), followed by heparin and fresh frozen plasma. Long term prophylaxis was LMW heparin or low dose warfarin plus stromba. The one patient who did not respond to the thrombolytic treatment with urokinase was found to have in his plasma a high titre of inhibitor against urokinase and prourokinase. This patient responded to streptokinase treatment. D-Dimer levels in these patients in non-crisis state were raised and proportional to the degree of the protein C deficiency.
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Alewine, Christine, Rebekah Landsman, Michael Rudloff, Emily Kolyvas, Jinqiu Chen, and Ira Pastan. "Abstract B37: Mesothelin-targeted immunotoxin RG7787 (LMB-100) preferentially depletes secreted proteins and short-lived intracellular proteins to augment tumor cell killing by taxanes." In Abstracts: AACR Special Conference on Pancreatic Cancer: Advances in Science and Clinical Care; May 12-15, 2016; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.panca16-b37.

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Breyer, H. G., R. Rahmanzadeh, P. Bacher, and B. Werner. "LMW-HEPARIN VERSUS HEPARIN-DHE IN ORTHOPAEDIC SURGERY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643689.

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The efficiancy and the side effects of a LMW heparin (FRAGMINR, KabiVitrum) and Heparin-DHE (Sandoz) have been compared in a randomized open prospective study of 120 patients (60/60) undergoing elective surgery on the lower limbs (total hip and knee replacement, corrective osteotomies). A radiofibrinogen uptake test (RFUT) was regularly done on all patients. Positive tests were controlled by ascending phlebography. The parameters, clinically obtained, included the intra-and postoperative blood loss, wound closure, and the incidence of haematoma. Hb, Hk, red and white blood cells, thrombocytes, total protein, aPTT, AT III, TT, and anti-Xy-activity were analyzed at the day before operation, the 2nd, 4th, and 6th day after operation.There were three positive RFUT in the group of LMW heparin (5 per cent), and there were six (10 per cent) in the control group. No pulmonary embolism occurred. In no case an operative treatment of deep vein thrombosis was done. There were no statistically significant differences in intra- and postoperative blood loss, and in the laboratory data, except the anti-Xa-activity, which was significantly higher in the LMW heparin group.The comparative study has shown, that a single daily injection of LMW heparin (FRAGMINR) is more effective than the two daily injections of the combination of UF heparin and DHE in order to prevent postoperative thromboembolism
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Higashiyama, S., I. Ohkubo, H. Ishiguro, and M. Sasaki. "A NEW FUNCTION OF HUMAN KININOGENS: THE AMINO-TERMINAL REGION OF DOMAIN 1 INVOLVES AN EF HAND-LIKE STRACTURE FOR METAL BINDING." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642851.

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Two types of kininogens in mammalian plasma, high molecular weight (HMW) and low molecular weight (LMW) kininogens, are the precursors of kinin. Especially, HMW kininogen circulates in the plasma as a complex with prekallikrein and factor XI, and functions as a cofactor in the initial phase reactions of intrinsic blood coagulation cascade. Recently, it has been found that the kininogens have inhibitory activity toward cysteine proteinases. The heavy chain portion, which is identical for HMW and LMW kininogens, is composed of three domains, domain 1, 2 and 3. Each the domain 2 and 3 has a reactive site as a cysteine proteinase inhibitor. However, physiological function of domain 1 remains still unknown. By using the antibody recognizing the interaction between HMW kininogen and Ca2+ (anti-HMW kininogen-Ca2+ antibody) as a probe, we newly found the Ca2+ binding site in the domain 1.Anti-HMW kininogen-Ca2+ antibody was isolated from anti-HMW kininogen antiserum as an antibody which bound to a HMW kininogen-Sepharose column equilibrated with 40 mM Tris-HCl buffer, pH 7.5, containing 1.0 M NaCl and 1 mM CaCl2, and was eluted with 3 mM EDTA. Resulting from the characterization by ELISA, this antibody specifically recognized the CB-1 region (CNBr-cleavage fragment 1: 1-160 amino acid sequence) of the heavy chain of kininogen molecules in the presence of Ca2+ or Mg2+. Furthermore, circular dichroism (CD) experiments showed that the conformational changes of HMW kininogen and heavy chain were induced by the addition of metal ions such as Ca2+ or Mg2+, and that this change was due to the conformational change of the CB-1 region. The dissociation constant (Kd) for heavy chain measured by Ca2+ titration analysis by CD at 214 nm was found to be 0.33 ± 0.09 mM. The number of Ca2+ binding sites of heavy chain calculated from Hill plot was 1.15 ± 0.04. The EF handlike structure found in the amino-terminal portion of the heavy chain of kininogen molecules strongly supported the above data. This indicates a possibility that kininogens play an important role as a Ca2+ binding protein.
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