The Reaction of Bovine Pancreatic Ribonuclease A with 6‐Chloropurineriboside 5′‐Monophosphate
Open Access
- 1 April 1980
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 105 (3), 571-579
- https://doi.org/10.1111/j.1432-1033.1980.tb04534.x
Abstract
The chemical modification of bovine pancreatic ribonuclease A by 6-chloropurine 9-β-d-ribo-furanosyl 5′-monophosphate was studied under several reaction conditions. The reaction, at pH 7.3, 40°C and a nucleotide: enzyme molar ratio of 60, showed a high degree of specificity in comparison to those corresponding to the base or the nucleoside. The main derivative was isolated by means of CM-cellulose chromatography. Subtilisin cleavage of this derivative showed that the substitution had taken place in the S-peptide moiety. Tryptic digestion of the S-peptide indicated that a lysine residue had been modified. Enzymatic and physico-chemical considerations showed that the actual site of reaction was the α-amino group of Lys-1. The structural and kinetic properties of the derivative are consistent with the existence of a phosphate-binding sub-site near the N-terminal region of the enzyme.This publication has 30 references indexed in Scilit:
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