Relevant bibliographies by topics / Gly-met

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  2. Dissertations / Theses
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  4. Conference papers

Academic literature on the topic 'Gly-met'

Author: Grafiati
Published: 4 June 2021
Last updated: 7 February 2022

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Journal articles on the topic "Gly-met"

1

Lau, Justin Kai-Chi, Seydina Lo, Junfang Zhao, K. W. Michael Siu, and Alan C. Hopkinson. "Fragmentation Chemistry of [Met-Gly]•+, [Gly-Met]•+, and [Met-Met]•+ Radical Cations." Journal of The American Society for Mass Spectrometry 24, no. 4 (February 26, 2013): 543–53. http://dx.doi.org/10.1007/s13361-013-0581-5.

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Barata-Vallejo, Sebastian, Carla Ferreri, Tao Zhang, Hjalmar Permentier, Rainer Bischoff, Krzysztof Bobrowski, and Chryssostomos Chatgilialoglu. "Radiation chemical studies of Gly-Met-Gly in aqueous solution." Free Radical Research 50, sup1 (October 25, 2016): S24—S39. http://dx.doi.org/10.1080/10715762.2016.1231402.

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GUANTIERI, V., A. M. TAMBURRO, D. CABROL, H. BROCH, and D. VASILESCU. "Conformational studies on polypeptide models of collagen. Poly(Gly-Pro-Val), poly(Gly-Pro-Met), poly(Gly-Val-Pro) and poly(Gly-Met-Pro)." International Journal of Peptide and Protein Research 29, no. 2 (January 12, 2009): 216–30. http://dx.doi.org/10.1111/j.1399-3011.1987.tb02248.x.

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4

Morozova, Olga B., Sergey E. Korchak, Hans-Martin Vieth, and Alexandra V. Yurkovskaya. "Photo-CIDNP Study of Transient Radicals of Met-Gly and Gly-Met Peptides in Aqueous Solution at Variable pH." Journal of Physical Chemistry B 113, no. 20 (May 21, 2009): 7398–406. http://dx.doi.org/10.1021/jp8112182.

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Jannatul, Ferdouse, Yuki Kusaba, Yuki Fujimaru, Yuki Yamamoto, and Hiroshi Kitagaki. "Methionine and Glycine Stabilize Mitochondrial Activity in Sake Yeast During Ethanol Fermentation." Food technology and biotechnology 57, no. 4 (2019): 535–43. http://dx.doi.org/10.17113/ftb.57.04.19.5665.

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Addition of amino acids to fermentation media affects the growth and brewing profiles of yeast. In addition, retaining mitochondrial activity during fermentation is critical for the fermentation profiles of brewer’s yeasts. However, a concrete mechanism linking amino acids in fermentation media with mitochondrial activity during fermentation of brewer’s yeasts is yet unknown. Here, we report that amino acids in fermentation media, especially methionine (Met) and glycine (Gly), stabilize mitochondrial activity during fermentation of sake yeast. By utilizing atg32Δ mutant sake yeast, which shows deteriorated mitochondrial activity, we screened candidate amino acids that strengthened the mitochondrial activity of sake yeast during fermentation. We identified Met and Gly as candidate amino acids that fortify mitochondrial activity in sake yeast during fermentation. To confirm this biochemically, we measured reactive oxygen species (ROS) levels in sake yeast fermented with Met and Gly. Yeast cells supplemented with Met and Gly retained high ROS levels relative to the non-supplemented sake yeast. Moreover, Met-supplemented cells showed a metabolome distinct from that of non-supplemented cells. These results indicate that specific amino acids such as Met and Gly stabilize the mitochondrial activity of sake yeast during fermentation and thus manipulate brewing profiles of yeast.
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Yamane, T., Y. Shiraishi, and T. Ashida. "Structure of Boc-Pro-Met-Gly-OBzl, C24H35N3O6S." Acta Crystallographica Section C Crystal Structure Communications 41, no. 6 (June 15, 1985): 946–50. http://dx.doi.org/10.1107/s0108270185006138.

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Brinkworth, Craig S., Tara L. Pukala, John H. Bowie, and Michael J. Tyler. "Host Defence Peptides from the Skin Glands of Australian Amphibians. Caerulein Neuropeptides and Antimicrobial, Anticancer, and nNOS Inhibiting Citropins from the Glandular Frog Litoria subglandulosa." Australian Journal of Chemistry 57, no. 7 (2004): 693. http://dx.doi.org/10.1071/ch03325.

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The host defence peptides from the skin secretions of the Australian Glandular Frog (Litoria subglandulosa) are similar to those of the closely related species Litoria citropa. Both species produce several potent caerulein neuropeptides and antimicrobial- and anticancer-active citropin peptides. The major neuropeptides from Litoria subglandulosa are caerulein 1.1 [pGlu Gln Asp Tyr(SO3) Thr Gly Trp Met Asp Phe–NH2], caerulein 1.2 [pGlu Gln Asp Tyr(SO3) Thr Gly Trp Phe Asp Phe–NH2], and caerulein 2.1 [pGlu Gln Asp Tyr(SO3) Thr Gly Ala His Met Phe–NH2], all of which are smooth muscle active. The major peptide, citropin 1.2 [Gly Leu Phe Asp Ile Ile Lys Lys Val Ala Ser Val Val Gly Gly Leu–NH2], is a wide-spectrum antibiotic and anticancer agent at the micromolar concentration. Citropin 1.2 also inhibits the formation of nitric oxide by the enzyme neuronal nitric oxide synthase (nNOS) at the micromolar concentration. Another peptide, citropin 2.2 [Gly Leu Ile Ser Ile Gly Lys Ala Leu Gly Gly Leu Ile Val Asp Val Leu Lys Pro Lys Ser–OH], also inhibits nNOS.
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Yong-Cun, Yang, Chi Shao-Ming, Liu Ming-Hua, Huang Rong, Wang Yu-Fei, Jing Bi, and Zhao Yan. "Spectrophotometric study of the selective binding behavior of aliphatic oligopeptides by bridged bis(β-cyclodextrin) linked by a 4,4′-diaminodiphenyl disulfide tether." Canadian Journal of Chemistry 88, no. 12 (December 2010): 1205–12. http://dx.doi.org/10.1139/v10-148.

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The conformation and binding behavior of 4,4′-diaminodiphenyl disulfide bridged bis(β-cyclodextrin) (1) towards representative aliphatic oligopeptides, i.e., Leu-Gly, Gly-Leu, Glu-Glu, Met-Met, Gly-Gly, Gly-Gly-Gly, and Gly-Pro, were investigated by circular dichroism, fluorescence, and 1H and 2D NMR spectroscopy at 25 °C in phosphate buffer (pH 7.20). The results indicated that 1 acts as an efficient fluorescent sensor and displays remarkable fluorescence enhancement upon addition of optically inert oligopeptides. Owing to the cooperative host–linker–guest binding mode in which the linker and guest are coincluded in the two cyclodextrin cavities, the bis(β-cyclodextrin) 1 gives high binding constants of up to 103–104 (mol/L)–1 for oligopeptides. The bis(β-cyclodextrin) 1 can recognize not only the size and shape of oligopeptides but also the hydrophobicity, giving an exciting residue selectivity of up to 61.3 for the Gly-Leu/Glu-Glu pair. These phenomena are discussed from the viewpoints of multiple recognition and induce-fit interactions between host and guest.
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Zhang, Jing-Bo, Yu-Qin Zhao, Yu-Mei Wang, Chang-Feng Chi, and Bin Wang. "Eight Collagen Peptides from Hydrolysate Fraction of Spanish Mackerel Skins: Isolation, Identification, and In Vitro Antioxidant Activity Evaluation." Marine Drugs 17, no. 4 (April 13, 2019): 224. http://dx.doi.org/10.3390/md17040224.

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A previous report indicated that collagen hydrolysate fraction (F7) from Spanish mackerel (Scomberomorous niphonius) skins showed high reducing power and radical scavenging activities on 2,2-Diphenyl-1-picrylhydrazyl (DPPH) (EC50 value of 1.57 mg/mL) and hydroxyl (EC50 value of 1.20 mg/mL). In this work, eight peptides were isolated from F7 and identified as Gly-Pro-Tyr (GPY, 335.31 Da), Gly-Pro-Thr-Gly-Glu (GPTGE, 459.47 Da), Pro-Phe-Gly-Pro-Asp (PFGPD, 531.52 Da), Gly-Pro-Thr-Gly-Ala-Lys (GPTGAKG, 586.65 Da), Pro-Tyr-Gly-Ala-Lys-Gly (PYGAKG, 591.69 Da), Gly-Ala-Thr-Gly-Pro-Gln-Gly (GATGPQG, 586.61 Da), Gly-Pro-Phe-Gly-Pro-Met (GPFGPM, 604.73 Da), and Tyr-Gly-Pro-Met (YGPM, 466.50 Da), respectively. Among them, PFGPD, PYGAKG, and YGPM exhibited strong radical scavenging activities on DPPH (EC50 values of 0.80, 3.02, and 0.72 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), hydroxyl (EC50 values of 0.81, 0.66, and 0.88 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), superoxide anion (EC50 values of 0.91, 0.80, and 0.73 mg/mL for PFGPD, PYGAKG, and YGPM, respectively), and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) cation (EC50 values of 0.86, 1.07, and 0.82 mg/mL for PFGPD, PYGAKG, and YGPM, respectively) in a positive concentration–activity relationship. Furthermore, PFGPD, PYGAKG, and YGPM could effectively reduce Fe3+ to Fe2+ and inhibit lipid peroxidation. Hence, eight collagen peptides from hydrolysate of Spanish mackerel skins might be served as antioxidant candidates for various industrial applications.
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Attia, Youssef A., Fulvia Bovera, Jinquan Wang, Mohammed A. Al-Harthi, and Woo Kyun Kim. "Multiple Amino Acid Supplementations to Low-Protein Diets: Effect on Performance, Carcass Yield, Meat Quality and Nitrogen Excretion of Finishing Broilers under Hot Climate Conditions." Animals 10, no. 6 (June 3, 2020): 973. http://dx.doi.org/10.3390/ani10060973.

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The objective of this study was to evaluate the effect of low-protein diets with amino acid supplementation on growth performance, carcass yield, meat quality and nitrogen excretion of broilers raised under hot climate conditions during the finisher period. In trial 1, broilers from 28 to 49 days of age were fed 18% crude protein (CP) as a positive control or 15% CP supplemented with (1) DL-methionine (Met) + L-lysine (Lys), (2) Met + Lys + L-Arginine (Arg), or (3) Met + Lys + L-Valine (Val). In trial 2, broilers from 30 to 45 days of age, were fed an 18% CP diet as a positive control or 15% CP supplemented with Met, Lys, Arg, Val, L-Isoleucine (Ile) or combination with glycine (Gly) and/or urea as nitrogen sources: (1) Met + Lys, (2) Met + Lys + Arg, (3) Met + Lys + Val, (4) Met + Lys + Ile, (5) Met + Lys + Arg +Val + Ile + Gly, and (6) Met+ Lys + Arg + Val + Ile + Gly + urea. Protein use was improved by feeding low-protein amino acid-supplemented diets as compared to the high-protein diet. Feeding 15% crude protein diet supplemented with only methionine and lysine had no negative effects on carcass yield, CP, total lipids and moisture% of breast meat while decreasing nitrogen excretion by 21%.
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Dissertations / Theses on the topic "Gly-met"

1

Jouini, Mohamed. "Etude physico-chimique de complexes peptidiques du cuivre (II) et du nickel (II) en solution." Paris 7, 1985. http://www.theses.fr/1985PA077054.

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Book chapters on the topic "Gly-met"

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Nabedryk, E., J. Breton, J. Wachtveitl, K. A. Gray, and D. Oesterhelt. "FTIR Spectroscopy of The P+Q A - /PQA State in Met L248→Thr, Ser L244→Gly, Phe M197→Tyr, Tyr M210→Phe, Tyr M210→Leu, Phe L181—Tyr and Phe L181—Tyr M210→Tyr L181—Phe M210 Mutants of RB. Shaeroides." In The Photosynthetic Bacterial Reaction Center II, 147–53. Boston, MA: Springer US, 1992. http://dx.doi.org/10.1007/978-1-4615-3050-3_18.

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Conference papers on the topic "Gly-met"

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Scheefers-Borchel, U., and G. Muller-Berghaus. "A NEW FIBRIN-SPECIFIC ANTIBODY DISCRIMINATING BETWEEN FIBRIN AND FIBRINOGEN IS DIRECTED AGAINST THE SYNTHETIC PEPTIDE LEU-ILE-ASP-GLY-LYS-MET." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643771.

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To determine soluble fibrin in blood of patients with coagulation disorders we produced monoclonal antibodies which distinct fibrin from fibrinogen and other blood constituents. Fibrin-specific monoclonal antibodies were obtained by immunizing mice with the synthetic hexapeptide Leu-Ile-Asp-Gly-Lys-Met which was covalently linked to KLH via its C-terminus. Several of the monoclonal antibodies which reacted with the hexapeptide also reacted with batroxobin-induced desAA-fibrin and thrombin-induced desAABB-fibrin, but not with fibrinogen. No reaction was observed with plasmin-induced fibrinogenolytic and fibrinolytic degradation products, respectively. The epitope recognized by these fibrin-specific antibodies is located on the αchain of fibrin and is not accessible for an antibody in native fibrinogen. One monoclonal antibody (B/H11) was used to quantify the amount of soluble fibrin in plasma of patients with a variety of coagulation disorders. This antibody could also be used to develop an ELISA based on two different fibrin-specific monoclonal antibodies. For this assay anti-fbn 17 (Scheefers- Borchel et al., Proc. Natl. Acad. Sci. USA 82: 7091, 1985) was coated onto ELISA plates. After adding plasma which contained soluble fibrin, the fibrin bound was detected by the second fibrin-specific antibody B/H^ to which biotin was covalently linked. The second antibody was probed by the addition of peroxydase conjugated streptavidin and the substrate ABTS for peroxydase. This test can be used to detect fibrin at concentrations as low as 70 ng/ml. With this assay system, it is possible to measure the amount of soluble fibrin present in plasma samples without the interference of fibrinogen which is associated with soluble fibrin.
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Sumi, Y., Y. Nakamura, M. Sakai, M. Muramatsu, and N. Aoki. "STRUCTURE OF HUMAN α2-PLASMIN INHIBITOR DEDUCED FROM THAT OF cDNA." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644371.

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The complete amino acid sequence of α2-plasmin inhibitor (α2PI) was determined by cDNA cloning. A Agt 10 cDNA library was prepared from poly(A)+mRNA isolated from cultured human liver cells. The labeled oligonucleotides, corresponding to the reported partial amino acid sequences of α2PI, were used as probes to screen the library. One of the positive clones was subcloned into plasmid pUC8. A 2.2 kilobase cDNA clone thus isolated contains a region coding for a portion of a leader sequence, the mature protein, a stop codon (TGA), a 3' noncoding region (733 nucleotides), and a poly(A)tail (37 nucleotides). The amino acid sequence deduced from the cDNA is composed of 452 amino acids starting with an amino-terminal sequence of Asn-Gln-Glu-Gln and ending with a carboxyl-terminal sequence of Gly-Ser-Pro-Lys. The sequence shows approximately 30% homology with those of other plasma serine protease inhibitors. However, α2PI extends 50-52 amino acids beyond the carboxyl-terminal ends of the other inhibitors. This 50-52 carboxyl-terminal amino acid sequence is therefore specific to α2PI, and contains the sequence that is exactly the same as that of the peptide containing the plasminogen binding site. There are three lysine residues possibly involved in the binding to plasminogen in this region. From the homology with the other inhibitors, the inhibitor's reactive-site peptide bond was suggested to be Met-Ser and the same as that of ai-antitrypsin. The Met residue is located at the 362 position from the amino-terminal end.
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Liu, Hua-zhen, Wei Chen, Qi-ying Liu, Xia Zhang, Li-xiu Wang, and Cheng-wu Chi. "A NEW PEPTIDE THROMBIN INHIBITOR FROM STREPTOMYCES GRISEUS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644330.

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A new peptide thrombin inhibitor was found in the Streptomyces griseus strain 254 isolated from a soil sample from Tongan, Fujian province, China, the inhibitor being a secondary metabolic product. The production of the inhibitor reached a maximum after 3 days culture of bacteria at 28°C in a rotary shaker. The inhibitor excreted in the culture filtrate was purified by absorption on macroporous resin, followed by ion exchange chromatography on DEAE-52, CM-32 cellulose, affinity chromatography on the immobilized thrombin and high performance liquid chromatography. The amino acid composition of the inhibitor was determined to be Val(2), Met(l), Ile(l), Leu(2) and Arg (1), similar to that of the amino acid residues around the reactive site of human antithrombin III, the critical plasma inhibitor of thrombin. The NH2-terminal residue of the inhibitor seems to be blocked by the alkyl group due to the negative reaction to ninhydrin, whereas the COO-terminal residue is most likely to be arginal because of that Arg was not found in the amino acid analysis, unless the peptide was oxidized by performic acid before acid hydrolysis. The chromogen substrates Bz-Phe-Val-Arg-PNA and Bz-Gly-Pro-Lys-PNA were used to determine the thrombin and plasmin activities, respectively. Besides thrombin, the purified inhibitor also exhibits a weak inhibitory activities on trypsin and much weak on plasmin, but not on chymotrypsin and other protein-ases.
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