The Reversible Reduction of Disulfide Bonds in Trypsin and Ribonuclease Coupled to Carboxymethyl Cellulose
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چکیده
منابع مشابه
The reversible reduction of disulfide bonds in trypsin and ribonuclease coupled to carboxymethyl cellulose.
It now seems very probable that the linear amino acid sequences of proteins are in some way uniquely determined by the sequence of nucleotides in the deoxyribonucleic acids of the chromosomes, or in the ribonucleic acids of some viruses. The simplest hypothesis regarding the control of the subsequent formation of three-dimensional configuration is that the amino acid sequence, alone, is suffici...
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In the course of an investigation of the chemical phosphorylation of ribonucleasel (cf. (l)), it became necessary to develop a chromatographic procedure for the fractionation of the phosphorylated protein. The method of Hirs et al. (2), employing the weak cation exchanger Amberlite XE-64, is an extremely valuable method for the chromatographic purification of pancreatic ribonuclease, but the us...
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The RNase molecule consists of a single chain, arranged in a compact, folded structure, cross-linked through 4 disulfide bridges (1). After hydrolysis to determine the amino acid composition of RNase, 8 half-cystine or cysteic acid residues have been identified (2,3) and the approximate location of these residues in the partial structural formula for oxidized RNase has been determined (4). More...
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15 صفحه اولRibonuclease A: Disulfide Bonds, Conformational Stability, and Cytotoxicity
Disulfide bonds between the side chains of cysteine residues are the only common crosslinks in proteins. Bovine pancreatic ribonuclease A (RNase A) is a 124-residue enzyme that contains four interweaving disulfide bonds (Cys26-Cys84, Cys40-Cys95, Cys58-CysllO, and Cys65-Cys72) and catalyzes the cleavage of RNA. The contribution of each disulfide bond to the confonnational stability and catalyti...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1962
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63414-9