The Reversible Reduction of Disulfide Bonds in Polyalanyl Ribonuclease
نویسندگان
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...
متن کاملThe relationship of disulfide bonds and activity in ribonuclease.
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...
متن کاملRibonuclease 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...
متن کاملDisulfide bonds are generated by quinone reduction.
The chemistry of disulfide exchange in biological systems is well studied. However, very little information is available concerning the actual origin of disulfide bonds. Here we show that DsbB, a protein required for disulfide bond formation in vivo, uses the oxidizing power of quinones to generate disulfides de novo. This is a novel catalytic activity, which to our knowledge has not yet been d...
متن کاملElectrolytic Reduction of the Disulfide Bonds of Insulin.
The role disulfides play in the stabilization of the secondary and tertiary structure of proteins has been of interest to protein chemists for some time. Despite the considerable amount of recently acquired knowledge about the mechanism of protein biosynthesis, no information is available concerning either the exact chemical nature of the process leading to the joining of the sulfhydryl groups ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1962
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)73943-x