منابع مشابه
Studies on Ribonuclease S
Specific regions of the polypeptide sequence of pancreatic ribonuclease have been altered by chemical modification and by limited proteolytic digestion in attempts to implicate specific covalent portions of the molecule in the structure and stabilization of the active center. Digestion of the native molecule with trypsin at elevated temperatures has been shown to remove portions of the chain wi...
متن کاملStudies on Ribonuclease S. I. Limited Carboxypeptidase Degradation of Ribonuclease S-protein and Ribonuclease S-peptide: Effects of Changes in Primary Structure on Enzymic Activity.
Specific regions of the polypeptide sequence of pancreatic ribonuclease have been altered by chemical modification and by limited proteolytic digestion in attempts to implicate specific covalent portions of the molecule in the structure and stabilization of the active center. Digestion of the native molecule with trypsin at elevated temperatures has been shown to remove portions of the chain wi...
متن کاملCrystalline semisynthetic ribonuclease-S'.
Crystals of solid phase-derived semisynthetic ribonuclease-S' were prepared and compared with those for native ribonuclease-S' and -S. The semisynthetic species used was the noncovalent complex of synthetic fragment-(1-20), corresponding to residues 1 through 20 of bovine pancreatic ribonuclease-A (ribonucleate 3'-pyrimidino-oligonucleotidohydrolase, EC 3.1.4.22), and native ribonuclease-S-(21-...
متن کاملStudies on the Antigenic Structure of Ribonuclease
Alkali-denatured bovine pancreatic ribonuclease (RNase) reacts poorly with antibody to the native molecule, and RNase whose disulfide bridges have been broken by oxidation or reduction is completely inactive with this antiserum. These observations suggest that the antigenicity of the native protein is, in part, attributable to its conformation (1). Oxidized RNase has no detectable immunogenic o...
متن کاملRibonuclease S redux.
The S-peptide and S-protein components of bovine pancreatic ribonuclease form a noncovalent complex with restored ribonucleolytic activity. Although this archetypal protein-fragment complementation system has been the object of historic work in protein chemistry, intrinsic limitations compromise its utility. Modern methods are shown to overcome those limitations and enable new applications.
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1964
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)91204-4