The Interaction of Subtilisin-modified Ribonuclease with Antisera against Native Ribonuclease
نویسندگان
چکیده
منابع مشابه
Abnormal tyrosine residues in subtilisin-modified ribonuclease.
Unfolding of the native conformation of pancreatic ribonuclease disrupts certain intramolecular associations of amino acids involving tyrosine residues (1) ; the subsequent absorbance changes serve as an index of the extent of denaturation of the enzyme (2). Of the 6 tyrosine residues of RNase A, 3 display distinct spectral properties which may be evaluated by determination of changes in ultrav...
متن کاملSubtilisin modification of monodeamidated ribonuclease-A.
Limited proteolysis of RNAase-Aa(1) (monodeamidated ribonuclease-A) by subtilisin results in the formation of an active RNAase-S type of derivative, namely RNAase-Aa(1)S. RNAase-Aa(1)S was chromatographically distinct from RNAase-S, but exhibited very nearly the same enzymic activity, antigenic conformation and susceptibility to trypsin as did RNAase-S. Fractionation of RNAase-Aa(1)S by trichlo...
متن کاملA Practical Preparation of Ribonuclease-S and the Action of Subtilisin on Ribonuclease-B ‡
All preparations of ribonuclease-S so far reported have employed limited digestion of ribonuclease-A with subtilisin,' a bacterial proteinase from B. subtilis described by Giintelberg and Ottesen.' The original supply of this latter enzyme is now exhausted. Another sample of a crystalline proteinase from B. subtilis (NOVO Enzyme) has been shown to differ from the original in several respects,' ...
متن کاملThe Preparation of Subtilisin-modified Ribonuclease and the Separation of the Peptide and Protein Components*
The proteolysis of bovine pancreatic ribonuclease by subtilisin has been shown to involve the formation of an enzymically active intermediate which is further degraded to inactive products (1, 2). This paper describes the preparation of the modified active ribonuclease, RNase (S)l and its fractionation into two components, a peptide (S-peptide) and a protein (S-protein). Neither S-peptide nor S...
متن کاملRegeneration of enzyme activity by air oxidation of reduced subtilisin-modified ribonuclease.
Fully reduced bovine ribonuclease, a molecule which probably exists in a random coil configuration (1, 2)) will, under the influence of molecular oxygen alone, oxidize to form an organized, enzymatically active product in high yield (3, 4). This material seems indistinguishable on the basis of physical properties from native ribonuclease (RNase) . These observations suggest that the information...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1959
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)69693-0