Archives of Pharmacal Research vol. 15, no. 3, pp. 229 - 233
Indexed
SCIE; SCOPUS; KCI
Document Type
Article
Abstract
The pKa value of histidine-51 residue was determined by the pH dependency of contents of NADH bound to the active site in the horse liver alcohol dehydrogenase and % inactivation with diethyl pyrocarbonate treatment of the enzyme. The pKa for His-51 was ~7.15 in the ternary complex and ~6.7 in the enzyme itself.