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Histochemistry and Cell Biology , 4 , Valuev, G. Sytov, I. Shanazarova, I. Valuev, Yu. Talyzenkov, N. Biodegradable polymeric derivatives of polypeptide drugs for targeting. Applied Biochemistry and Microbiology , 44 2 , Analytical Biochemistry , 2 , Journal of Bioactive and Compatible Polymers , 11 2 , Andry, M. Determination of free amino group content of serum albumin microcapsules using trinitrobenzenesulfonic acid: effect of variations in polycondensation pH.
International Journal of Pharmaceutics , 96 , The molybdoenzymes xanthine oxidase and aldehyde oxidase contain fast- and slow-DTNB reacting sulphydryl groups. Journal of Protein Chemistry , 11 5 , Roig, John F. Nonstarch polysaccharides and the texture of french fried potato. Kakade, M. A simplified procedure for the determination of availabale lysine in protein and protein foodstuffs.
Mauron, J. Progress in meeting protein needs of infants and preschool children. Muller, E. Effect of nitrogen, phosphorus, potassium and magnesium nutrition of potato plants on the content of free amino acids and on the amino acid composition of the protein of the tubers. Plant and Soil 7: — Osner, R.
Nutritional changes in proteins during heat processing. Reynolds, T. Chemistry of non-enzymatic browning II. Data availability:. Record : found Abstract : not found Article : not found. Download citation. Received : 11 February Issue Date : August Search SpringerLink Search. Abstract Guanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification.
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Biochemistry , 8 9 , 01 Sep Cited by 9 articles PMID: J Chromatogr , 32 2 , 01 Jan Cited by 4 articles PMID: Anal Biochem , 19 2 , 01 May Cited by 7 articles PMID: Cohen LA. Annu Rev Biochem , , 01 JanGuanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification. Decreases in thermal stability result from greater modification. These results support suggestions that surface guanidino groups arginyl groups are an important factor in thermal stability of proteins. This is a preview of subscription determination of free amino groups in proteins by trinitrobenzenesulfonic acid, log in to check access. Rent this article via DeepDyve. Ljungdahl LG: Physiology of thermophilic bacteria. Adv Microbiol Physiol —, Google Scholar. Williams RAO: Caldoactive and thermophilic bacteria and their determination of free amino groups in proteins by trinitrobenzenesulfonic acid proteins. Sci Prog Oxford —, Birkhauser Verlag, Basel,pp — Int J Pept Protein Res —, Wolfenden R: Waterlogged molecules. Science —, Determination of free amino groups in proteins by trinitrobenzenesulfonic acid Biochem Biophys —, J Biol Chem —, Biochemistry —, J Inorg Biochem —82, Racker E: Alcohol dehydrogenase from baker's yeast. Meth Enzymol —, Worthington Biochemical Co. Bradford MM: A rapid and sensitive method for the quantitation final destination 1 full movie in hindi watch online free microgram quantities of protein utilizing the principle of protein-dye binding. BIOCHEMISTRY. 14, (). Determination of Free Amino Groups in Proteins by Trinitrobenzenesulfonic. Acid. A. F. S. A. HABEEBl. From the Clinical. Determination of Free Amino Groups in Proteins by Trinitrobenzenesulfonic Acid. Anal Biochem. Mar;14(3) doi: /(66) Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. for the photometric determination of amino acids and related compounds. PDF | Trinitrobenzenesulfonic acid (TNBSA) is the reagent in a The TNBSA method is also fre- determining the quantity of alkylated lysine in protein tion of the primary amino groups of proteins to deter- agent, and there The sulﬁte-free TNP–amine absorbs at nm solve the problem of repeatability. amino groups.1 Primary amines, upon reaction with TNBSA, form a highly Determination of free amino groups in protein by trinitrobenzene sulfonic acid. Anal. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Authors: A.F.S.A. Habeeb. Publication date Created: March Publication. applied to the determination of protein, the detection limit was g/assay for BSA. Satisfactory recovery Keywords: glutaraldehyde, XTT, amino group, amino acid, protein, milk food protein hydrolysates by trinitrobenzenesulfonic acid. J. Agric. phonic acid (TNBS) as a reagent for free epsilon amino group of lysine. Two modified versions of the trinitrobenzene sulfonic acid. (TNBS) procedure for the determination of free amino groups in proteins (AFSA Habeeb, Anal. Determination of free amino groups in protein by trinitrobenzene sulfonic acid. Anal Biochem Hermanson, G. (). Bioconjugate Techniques, p Determination of free amino group content of serum albumin microcapsules using trinitrobenzenesulfonic acid: effect of variations in polycondensation pH. Amino acids that have secondary amino group attachments also react with ninhydrin. The essential groups of lysozyme, with particular reference to its reaction with iodine. The major modification from previous procedures is an extended TNBS reaction time to allow a stoichiometric reaction with amino groups. Tertiary structure of ribonuclease. Copyright and License information Disclaimer. They are soluble in water but not in nonpolar organic solvents such as cyclohexane. The amino acid phenylalanine also contains a benzene ring, but the ring is not activated and, therefore, does not readily undergo nitration. A procedure using 2,4,6-trinitrobenzenesulfonic acid TNBS for the determination of epsilon-amino groups in soluble and poorly soluble proteinaceous materials is presented. Oxygen toxicity, oxygen radicals, transition metals and disease. This nitration reaction, when used to identify the presence of an activated benzene ring, is commonly known as the xanthoproteic test, because the product is yellow. Covalent labeling of active sites. Associated Data Supplementary Materials. Free amino groups were analyzed in the water-insoluble fraction WIF of cataractous human lenses of the nuclear sclerosis, pigmented type. Dissociation constants of the guamidinium ion and of some amino acids.