Academic literature on the topic 'Protein Preparation'

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Journal articles on the topic "Protein Preparation"

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Pęksa, A., and J. Miedzianka. "Amino acid composition of enzymatically hydrolysed potato protein preparations." Czech Journal of Food Sciences 32, No. 3 (2014): 265–72. http://dx.doi.org/10.17221/286/2013-cjfs.

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We determine the effects of the technology of obtaining potato protein preparation and of different variants of enzymatic hydrolysis on the chemical and amino acid compositions of the hydrolysates obtained. Potato protein concentrates obtained through their thermal coagulation in potato juice with calcium chloride, calcium lactate or without salt addition were subjected to enzymatic hydrolysis using two commercial hydrolytic enzymes: endopeptidase (Alcalase) and exopeptidase (Flavourzyme). Chemical (contents of ash, total and coagulable protein) and amino acid compositions of the hydrolysates
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Semenova, I. B., and N. A. Mikhailova. "SEROTYPE-INDEPENDENT VACCINES AGAINST PNEUMOCOCCAL INFECTION." Journal of microbiology, epidemiology and immunobiology, no. 4 (August 28, 2016): 76–85. http://dx.doi.org/10.36233/0372-9311-2016-4-76-85.

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Creation of serotype-independent vaccines includes 4 directions - construction of protein vaccines based on recombinant pneumococcus proteins, whole-cell killed or attenuated vaccines, DNA-vaccines and use of Streptococcus pneumoniae as a carrier for polysaccharide and conjugated vaccine preparations. Protein vaccines are the most widely studied. Around 20 proteins are described for pneumococcus - intracellular, associated with cell wall and secreted. The majority of researchers stop at construction of a vaccine preparation including a set of several proteins, protecting from colonization, inv
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Chazot, J. A., and P. G. Strange. "Coupling of D2 dopamine receptors to G-proteins in solubilized preparations of bovine caudate nucleus." Biochemical Journal 281, no. 2 (1992): 369–75. http://dx.doi.org/10.1042/bj2810369.

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1. The coupling of D2 dopamine receptors and G-proteins has been examined in cholate-solubilized preparations of bovine caudate nucleus. 2. No receptor-G-protein coupling could be detected in solubilized preparations obtained in 0.3% cholate, but if this preparation is diluted 5-fold, coupling is re-established. 3. The dilution process was examined, and it was shown that the change in ionic strength was an important factor in modulating the observed receptor-G-protein interaction. 4. Ionic strength was shown, however, not to be the primary determinant of receptor-G-protein coupling. This is li
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Shaginova, L. O., I. V. Krylova, T. F. Demianenko, and M. L. Domoroshchenkova. "Study of a process of obtaining of protein preparation from sunflower seeds for application in food industry." New Technologies 17, no. 3 (2021): 41–50. http://dx.doi.org/10.47370/2072-0920-2021-17-3-41-50.

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The article deals with a study of processing methods of obtaining protein preparations from sunflower seeds. For obtaining of food-grade protein preparations from the defatted sunflower kernels phenolic compounds were additionally removed. Modern Russian and foreign literature sources devoted to the isolation of phenolic compounds from vegetable protein raw materials were analyzed. The objective of obtaining a light-colored food-grade protein preparation from sunflower seeds was solved through developing of a multi-stage extraction process with removal of various groups of non-protein compound
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Cohen, D. C., and P. T. Doyle. "Effect of sample preparation on in situ estimates of protein degradability for white clover herbages." Australian Journal of Experimental Agriculture 41, no. 5 (2001): 619. http://dx.doi.org/10.1071/ea00168.

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The amount of crude protein in white clover solubilised during ingestion by cows was determined by collecting swallowed boluses in rumen fistulated cows. Six experiments were then conducted to determine the effects of sample preparation on in situ estimates of rumen degradability of crude protein in white clover (Trifolium repens L.) herbages. Different methods of preparation were compared with chopped fresh herbage, a recommended method when this type of feed is incubatedin situ. Samples of white clover were either: (i) chopped fresh to 10 mm lengths (FRS), (ii) frozen, freeze-dried and groun
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Pahud, Jean‐Jacques, Julio César Monti, and Rolf Jost. "Allergenicity of Whey Protein." Journal of Pediatric Gastroenterology and Nutrition 4, no. 3 (1985): 408–13. http://dx.doi.org/10.1002/j.1536-4801.1985.tb08871.x.

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Enzymatic in vitro hydrolysis was evaluated as a possible treatment to abolish the allergenicity of whey proteins in view of their use in infant formulas. Guinea pigs without prior immunological contact (including fetal life) with cow'S milk were fed various preparations of cow'S milk proteins. Oral exposure to milk or untreated whey protein led to anaphylactic sensitization of the animals. In contrast, trypsin‐hydrolyzed whey protein and a peptide preparation produced from the tryptic hydrolysate by ultrafiltration were devoid of sensitizing capacity by the oral route. The hydrolysate (crude
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Toru-Delbauffe, D., M. Pierre, J. Osty, F. Chantoux, and J. Francon. "Properties of neurofilament protein kinase." Biochemical Journal 235, no. 1 (1986): 283–89. http://dx.doi.org/10.1042/bj2350283.

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Neurofilament (NF) protein kinase, partially purified from NF preparations [Toru-Delbauffe & Pierre (1983) FEBS Lett. 162, 230-234], was found to be distinct from both the casein kinase present in NFs and the cyclic AMP-dependent protein kinase which is able to phosphorylate NFs. NF-kinase phosphorylated the three NF protein components. The amount of phosphate incorporated per molecule was higher for NF 200 than for NF 145 and NF 68. Other proteins present in the NF preparations were also used as NF-kinase substrates. Two of them might correspond to the myelin basic proteins with Mr values
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Meyer,, Kevin. "Automating Protein Sample Preparation." Genetic Engineering & Biotechnology News 31, no. 1 (2011): 28–29. http://dx.doi.org/10.1089/gen.31.1.14.

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Schotters, S. B., J. H. McBride, D. O. Rodgerson, S. Higgins, and M. Pisa. "Standardization for four protein analytes with the Behring Nephelometer." Clinical Chemistry 34, no. 9 (1988): 1870–72. http://dx.doi.org/10.1093/clinchem/34.9.1868.

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Abstract Owing to the generally higher values observed in the initial establishment of immunoglobulins (Ig) G, A, and M assays with the Behring Nephelometer, we elected to verify five commercial protein calibrators. This initial verification was performed by standardizing the Behring Nephelometer with the World Health Organization (WHO) International Reference Preparation for Human Serum Immunoglobulins G, A, and M. The instrument was also standardized for immunoglobulins and transferrin with use of the Reference Preparation for Serum Proteins (RPSP II). Analytical recoveries of the commercial
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Cheng, Hao-Tsai, Sen-Yung Hsieh, Chang-Mu Sung, Betty Chien-Jung Pai, Nai-Jen Liu, and Carl PC Chen. "Optimizing Human Bile Preparation for Two-Dimensional Gel Electrophoresis." BioMed Research International 2016 (2016): 1–6. http://dx.doi.org/10.1155/2016/5185317.

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Aims. Bile is an important body fluid which assists in the digestion of fat and excretion of endogenous and exogenous compounds. In the present study, an improved sample preparation for human bile was established.Methods and Material. The method involved acetone precipitation followed by protein extraction using commercially available 2D Clean-Up kit. The effectiveness was evaluated by 2-dimensional electrophoresis (2DE) profiling quality, including number of protein spots and spot distribution.Results. The total protein of bile fluid in benign biliary disorders was 0.797 ± 0.465 μg/μL. The sa
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Dissertations / Theses on the topic "Protein Preparation"

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Guzman-Juarez, M. "Yeast protein products : Preparation, characterisation and functional properties." Thesis, University of Reading, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.376661.

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Christie, Patricia Dianne 1967. "Preparation of isotopically labeled MoFe protein of nitrogenase." Thesis, Massachusetts Institute of Technology, 1996. http://hdl.handle.net/1721.1/11229.

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Alzahrani, Eman Saad. "Investigation of monolithic materials for protein sample preparation." Thesis, University of Hull, 2012. http://hydra.hull.ac.uk/resources/hull:7149.

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Proteomics plays an important role in the recognition of diseases and the understanding of biological processes. Sample preparation is a bottleneck in systems for chemical analysis and it is a required step in proteomics in order to remove interferences and preconcentrate the proteins. In addition, protein reduction and alkylation before digestion is a required step in proteomics to facilitate protein unfolding and increase the efficiency of enzymes in digesting proteins. The purpose of this study was to develop new techniques to address some of the shortcomings of current sample preparation m
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Shiozaki, Aiko. "Proteome analysis of brain proteins in Alzheimer's disease : Subproteomics following sequentially extracted protein preparation." Kyoto University, 2004. http://hdl.handle.net/2433/147486.

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Moosavi-Nasab, Marzieh. "Protein structural changes during preparation and storage of surimi." Thesis, McGill University, 2003. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=84297.

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Myofibrillar proteins, the main components that impart functional properties to muscle foods, can undergo denaturation and aggregation during frozen storage. The overall objective of this research was to study the changes in protein structure that are associated with the preparation and frozen storage of surimi. In addition, the relative cryoprotective effects of whey protein concentrate, whey protein isolate, soy protein isolate, flaxseed meal and flaxseed protein were assessed in surimi during storage.<br>Raw surimi was prepared by repeatedly washing Alaska pollock flesh with chilled
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Kittivoravitkul, Sasitorn. "Preparation, characterisation and in vivo evaluation of DHEA protein conjugates." Thesis, University College London (University of London), 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250667.

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GÓMEZ, PÉREZ INMACULADA JÉNNIFER. "DESIGN AND PREPARATION OF CARBON NANODOTS FOR BIOMEDICAL APPLICATIONS." Doctoral thesis, Università degli Studi di Trieste, 2018. http://hdl.handle.net/11368/2919821.

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In the last few decades great efforts have been placed in studying carbon nanomaterials. Nowadays the nanocarbon family spans from fullerene, the first member, to Carbon Dots (C-Dots), the last to join. C-Dots have attracted considerable attention for a wide range of applications, especially bioapplications, because of their properties: emission, small sizes, aqueous solubility, biocompatibility and chemical stability. The aim of this doctoral thesis was to synthesize Carbon nanodots (CNDs), in particular nitrogen-doped CNDs, and functionalize their surface with properly designed molecules/bio
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Cervantes-Laurean, Daniel. "Preparation and Characterization of Model Conjugates for the Study of Proteins Modified by ADP-ribose." Thesis, University of North Texas, 1992. https://digital.library.unt.edu/ark:/67531/metadc935701/.

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Modification of proteins by ADP-ribose has been shown to be a versatile modification with respect to the amino acid side chain. The results described here will allow the study of the biological importance of ADP-ribose glycation and also allow differentiation on crude extracts between enzymatic modifications from protein ADP-ribose glycation that can occur due to the presence of NAD glycohydrolases.
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Jansson, Eva. "Blood protein coated model biomaterials : preparation, and cell and tissue response /." Linköping : Univ, 2003. http://www.bibl.liu.se/liupubl/disp/disp2003/tek798s.pdf.

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Calvert, Elaine. "Preparation and characterisation of a multichain protein from the wool microfibril." Thesis, University of Leeds, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.235590.

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Books on the topic "Protein Preparation"

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Alexander, McPherson. Preparation and analysis of protein crystals. 2nd ed. R.E. Krieger Pub. Co., 1989.

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1951-, Kamp R. M., Choli-Papadopoulou T. 1956-, and Wittmann-Liebold B. 1931-, eds. Protein structure analysis: Preparation, characterization, and microsequencing. Springer, 1997.

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Dahir, Nadheim D. Technetium-99m-dimercaptosuccinic acid complexes: Preparation and plasma protein-binding studies. University of Birmingham, 1988.

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N, Berry Michael, Edwards A. M, and Barritt Gregory J, eds. Laboratory techniques in biochemistry and molecular biology.: Preparation, properties, and applications. Elsevier, 1991.

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Mathieu, Melissa G. Preparation and preliminary characterization of human adrenal cells expressing dominant inhibitory mutations in protein kinase A. Laurentian University, Department of Biology, 2000.

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Kānphǣt, Thailand Krom Witthayāsāt. Rāingān kānpramœ̄n khwāmplō̜tphai Sūn Pramœ̄n Khwāmsīang læ Čhǣng Tư̄an Phai, Krom Witthayāsāt Kānphǣt =: Ice structuring protein preparation (glacein) ISP, Risk Assessment Center, Department of Medical Sciences. Krom Witthayāsāt Kānphǣt, Krasūang Sāthāranasuk, 2007.

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Rakosky, Joseph. Protein additives in foodservice preparations. Van Nostrand Reinhold, 1989.

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Spada, Stefania. Directory of approved biopharmaceutical products. CRC Press, 2005.

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Hagen, Jörg von. Proteomics sample preparation. Wiley-VCH, 2008.

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Staby, Arne, Anurag S. Rathore, and Satinder Ahuja, eds. Preparative Chromatography for Separation of Proteins. John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781119031116.

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Book chapters on the topic "Protein Preparation"

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Hayter, Roy. "Vegetables, rice and vegetable protein." In Food Preparation and Cooking. Macmillan Education UK, 1992. http://dx.doi.org/10.1007/978-1-349-13181-5_17.

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Harvey, David J. "Enzymatic Preparation and Isolation of Glycopeptides." In Protein Sequencing Protocols. Humana Press, 2003. http://dx.doi.org/10.1385/1-59259-342-9:83.

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Shahidi, F. "Seafood proteins and preparation of protein concentrates." In Seafoods: Chemistry, Processing Technology and Quality. Springer US, 1994. http://dx.doi.org/10.1007/978-1-4615-2181-5_2.

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He, Zengyou, Ting Huang, Can Zhao, and Ben Teng. "Protein Inference." In Modern Proteomics – Sample Preparation, Analysis and Practical Applications. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-41448-5_12.

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Benotti, Peter N. "Nutrition I: Protein and Vitamins." In Patient Preparation for Bariatric Surgery. Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-0906-3_7.

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Turriziani, Benedetta, Alexander von Kriegsheim, and Stephen R. Pennington. "Protein-Protein Interaction Detection Via Mass Spectrometry-Based Proteomics." In Modern Proteomics – Sample Preparation, Analysis and Practical Applications. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-41448-5_18.

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Cook, Elizabeth A., and Mingyue He. "Preparation of Protein Arrays Using Cell-Free Protein Expression." In Methods in Molecular Biology. Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-782-2_16.

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Minegishi, Seiji, Taro Saito, and Shin-ichi Hisanaga. "Cyclin-Dependent Kinase 5 (Cdk5): Preparation and Measurement of Kinase Activity." In Protein Kinase Technologies. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-824-5_6.

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Paternostre, Maïté, Michel Ollivon, and Jacques Bolard. "Liposomes: Preparation and Membrane Protein Reconstitution." In Manual on Membrane Lipids. Springer Berlin Heidelberg, 1996. http://dx.doi.org/10.1007/978-3-642-79837-5_9.

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Taylor, Justine, Can Wang, and D. Jed Harrison. "Multiplexed Protein Preparation Systems for Proteomics." In Micro Total Analysis Systems 2002. Springer Netherlands, 2002. http://dx.doi.org/10.1007/978-94-010-0295-0_115.

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Conference papers on the topic "Protein Preparation"

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Tyumentsev, A. I., M. A. Tyumentseva, and V. G. Akimkin. "DEVELOPMENT OF APPROACHES FOR ENDOTOXIN REMOVAL FROM PROTEIN PREPARATIONS ON THE EXAMPLE OF NUCLEASES OF THE CRISPR/CAS SYSTEM." In Molecular Diagnostics and Biosafety. Federal Budget Institute of Science 'Central Research Institute for Epidemiology', 2020. http://dx.doi.org/10.36233/978-5-9900432-9-9-113.

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Removal of bacterial endotoxins from solutions of recombinant proteins is one of the most important issues in the preparation of highly purified preparations suitable for in vivo use. An optimal technology for obtaining preparations purified from bacterial endotoxins has been proposed using purification of preparations of recombinant nucleases of the CRISPR/CAS system as an example. Efficacy of developed technology was compared with other available methods. Removal of bacterial endotoxins was carried out using Triton X-114 detergent added to a concentration of 1% to a solution containing the r
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XiHuai Qiang and Hongyan Feng. "Preparation of protein-surfactant with waste feather." In 2011 International Conference on Remote Sensing, Environment and Transportation Engineering (RSETE). IEEE, 2011. http://dx.doi.org/10.1109/rsete.2011.5965769.

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Wilkinson, J. M., N. Hack, L. I. Thorsen, and J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.

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Platelet membrane preparations can be fractionated into two major subpopulations by free flow electrophoresis and these have been shown to correspond to the plasma membrane and the endoplasmic reticulum of the platelet. The plasma membrane fraction can be shown, by two-dimensional electrophoresis, to contain the major surface glycoproteins together with considerable amounts of actin and actin-associated proteins such as the 250 kDa actin-binding protein (filamin), P235 (talin), myosin, α-actinin and tropomyosin (Hack, N. … Crawford, N., Biochem. J. 222, 235 (1984). These cytoskeletal proteins
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Simion, Monica, Lavinia Ruta, Irina Kleps, et al. "Biohybrid surface preparation for protein/DNA microarray applications." In 2008 International Semiconductor Conference. IEEE, 2008. http://dx.doi.org/10.1109/smicnd.2008.4703368.

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Xiaoju Zhang and Shijie Li. "Preparation and characterization of polysaccharide/ protein biodegradable membrane." In 2011 Second International Conference on Mechanic Automation and Control Engineering (MACE). IEEE, 2011. http://dx.doi.org/10.1109/mace.2011.5987459.

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Schreiber, A. B., R. Gillette, and M. E. Hrinda. "IN VITRO IMMUNE PARAMETERS OF MONOCLATEH, A, MONOCLONAL ANTIBODY PURIFIED HUMAN PLASMA FACTOR VIII:C THERAPEUTIC PREPARATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644051.

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MonoclateR is a highly purified human factor VIII:C preparation obtained by immunoaffinity chromatography of plasma cryoprecipitat followed by chromatography on aminohexyl sepharose. The resulting product is devoid of alloantigens, can be stabilized in the absence of extraneous human proteins and has a specific activity higher than 3000 U/mg.To ascertain product integrity, we set out to compare MonoclateR preparations with either unfractionated human plasma, cryoprecipitateor commercially available lyophilized antihemophilia factor (AHF) preparations by Western blots. As probes, we utilized a
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Tseng, Fan-Gang. "From High Performance Protein Micro Chip Toward Ultra High Sensitive Single Molecule Nano Array." In ASME 2009 7th International Conference on Nanochannels, Microchannels, and Minichannels. ASMEDC, 2009. http://dx.doi.org/10.1115/icnmm2009-82291.

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Protein microarrays have been employed to screen tens to thousands of proteins simultaneously for the observation of the biochemical activities in the protein-protein, protein-nucleic acid and small molecule interactions. This technology allows high throughput analysis and holds great potential for basic molecular biology research, disease marker identification, toxicological response profiling and pharmaceutical target screening. However, proteins easily malfunction in harsh environments so that they are hardly preserved before the application because of their complex and fragile structures.
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Anwar, Khalid, Taeheon Han, and Sun Min Kim. "An Integrated Micro/Nanofluidic System for Processing of Protein Samples." In ASME-JSME-KSME 2011 Joint Fluids Engineering Conference. ASMEDC, 2011. http://dx.doi.org/10.1115/ajk2011-36036.

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In this study, an integrated micro/nanofluidic system for protein analysis was presented. The device is comprised of a micromixer and a preconcentrator with a separation column. The integrated micromixer based on unbalanced split and cross collision of fluid streams is passive and planar, which is easy to fabricate and integrate to the microfluidic system. The preconcentrator has nanochannels formed by the electrical breakdown of polydimethylsiloxane (PDMS) membrane using a high electrical shock, without any nano-lithographic process. Micromixer and preconcentrator were used for sample prepara
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Zhang, Yue-hong, Qing Shang, Ting Zheng, Yuan-yuan Liang, and Tong Chen. "Preparation of pH-sensitive Hydrogels for Oral Delivery of Protein." In 2012 International Conference on Biomedical Engineering and Biotechnology (iCBEB). IEEE, 2012. http://dx.doi.org/10.1109/icbeb.2012.310.

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Omelchenko, M. M., O. P. Boiko, V. G. Nazarenko, R. O. Vlokh, and Yu A. Nastishin. "Alignment techniques for preparation of protein-containing surfactant nematic cells." In European Conference on Biomedical Optics, edited by Dietrich Schweitzer and Maryann Fitzmaurice. SPIE, 2007. http://dx.doi.org/10.1117/12.727654.

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Reports on the topic "Protein Preparation"

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Veen, Ryan Vander, Mark Mogler, Matthew M. Erdman, and D. L. Hank Harris. Preparation of GP5-M Heterodimer Glycantype Specific Recombinant Protein and Replicon Particles. Iowa State University, 2009. http://dx.doi.org/10.31274/ans_air-180814-698.

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Gafni, Yedidya, and Vitaly Citovsky. Molecular interactions of TYLCV capsid protein during assembly of viral particles. United States Department of Agriculture, 2007. http://dx.doi.org/10.32747/2007.7587233.bard.

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Tomato yellow leaf curl geminivirus (TYLCV) is a major pathogen of cultivated tomato, causing up to 100% crop loss in many parts of the world. The present proposal, a continuation of a BARD-funded project, expanded our understanding of the molecular mechanisms by which CP molecules, as well as its pre-coat partner V2, interact with each other (CP), with the viral genome, and with cellular proteins during assembly and movement of the infectious virions. Specifically, two major objectives were proposed: I. To study in detail the molecular interactions between CP molecules and between CP and ssDN
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Karnchanatat, Aphichart. Fibrinolytic enzyme from Sand Warm Perinereis nuntia. Chulalongkorn University, 2013. https://doi.org/10.58837/chula.res.2013.106.

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A protease from sandworms (Perinereis nuntia) was purified by using a combination of ammonium sulfate precipitation, DEAE cellulose and Superdex-200, respectively. The enriched preparation had a specific activity of 355.74 U/mg proteins and a yield of 18.5% total protein. The molecular weight of this protease was estimated to be 37.4 kDa by SDS-15% (w/v) PAGE. The pH stability of this protease is between pH 7-8, and it is stable up to 40 °C. The activity of the enzyme was inhibited by Cu2+ and Co2+, but was enhanced by Ca2+ and Mg2+ ions. Furthermore, protease activity was potently inhibited b
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Pawlowski, David R. Automated Sample Preparation (ASP): Development of a Rapid Method to Sequentially Isolate Nucleic Acids and Protein from Any Sample Type by a Cartridge-Based System. Defense Technical Information Center, 2013. http://dx.doi.org/10.21236/ada608052.

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Pirone, Thomas P., Benjamin Raccah, and Nor Chejanovsky. Vector Specificity in Potyvirus Transmission: Role of the Helper Component. United States Department of Agriculture, 2003. http://dx.doi.org/10.32747/2003.7586456.bard.

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Objectives: The overall objective of this research was to gain a better understanding of how potyviruses interact with their aphid vectors. The aim was to design new approaches for prevention of potyvirus spread by aphids. The sub-objectives included: (1). Determination of which of the HCs of different potyviruses effect efficient transmission by specific aphid vectors; (2). Determine regions in the HC that play a role in their compatibility with the vector; (3). Determine the factors within the aphid stylets that modify HC activity in transmission. Background of the topic: Background to the t
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Nelson, Nathan, and Charles F. Yocum. Structure, Function and Utilization of Plant Photosynthetic Reaction Centers. United States Department of Agriculture, 2012. http://dx.doi.org/10.32747/2012.7699846.bard.

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Light capturing and energy conversion by PSI is one of the most fundamental processes in nature. In the heart of these adaptations stand PSI, PSII and their light harvesting antenna complexes. The main goal of this grant proposal was to obtain by X-ray crystallography information on the structure of plant photosystem I (PSI) and photosystem II (PSII) supercomplexes. We achieved several milestones along this line but as yet, like several strong laboratories around the world, we have no crystal structure of plant PSII. We have redesigned the purification and crystallization procedures and recent
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Ueti, Massaro Wilson, and Monica Leszkowicz Mazuz. Identification, characterization and testing of geographically conserved Babesia bovis vaccine antigen candidates. United States-Israel Binational Agricultural Research and Development Fund, 2022. http://dx.doi.org/10.32747/2022.8134143.bard.

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During the development of this project, we selected four potential B. bovis antigens for a subunit vaccine to prevent the clinical signs of acute bovine babesiosis. Selection of the target antigens was based on: (1) profile of expression in parasite blood stages; (2) prediction for protein location on the parasite surface and/or on the surface of infected red blood cells; and (3) target conservation between US and Israeli strains of B. bovis. Following these criteria, the B. bovis targets BBOV_IV009170, BBOV_III007410, BBOV_II001790, and BBOV_III008720 were selected. Full-length genomic sequen
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Yedidia, I., H. Senderowitz, and A. O. Charkowski. Small molecule cocktails designed to impair virulence targets in soft rot Erwinias. United States-Israel Binational Agricultural Research and Development Fund, 2020. http://dx.doi.org/10.32747/2020.8134165.bard.

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Chemical signaling between beneficial or pathogenic bacteria and plants is a central factor in determining the outcome of plant-microbe interactions. Pectobacterium and Dickeya (soft rot Erwinias) are the major cause of soft rot, stem rot, and blackleg formed on potato and ornamentals, currently with no effective control. Our major aim was to establish and study specific bacterial genes/proteins as targets for anti-virulence compounds, by combining drug design tools and bioinformatics with experimental work. The approach allowed us to identify and test compounds (small molecules) that specific
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Shemon, Emily R. Preparation for a PROTEUS Software Quality Assurance Plan. Office of Scientific and Technical Information (OSTI), 2018. http://dx.doi.org/10.2172/1483832.

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Walker, Michael, Gill Holcombe, Clare Mills, Chiara Nitride, and Adrian Rogers. Development of Reference Materials for food allergen analysis. Food Standards Agency, 2023. http://dx.doi.org/10.46756/sci.fsa.hwt621.

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Food hypersensitivity is an increasing problem for many stakeholders with much effort focused on assessment and management of the risks including risk assessment toolkits (for example, the Allergen Bureau (Opens in a new window) Voluntary Incidental Trace Allergen Labelling VITAL®, the iFAAM consortium (Opens in a new window) and the ILSI-Europe Allergen Quantitative Risk Assessment guidance (Opens in a new window)). These toolkits describe the use of action levels and reference doses to assess the risks. A combination of the estimated eliciting dose of allergenic food, (in milligrams as prote
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