Abstract
The amino acid composition of octopine dehydrogenase from muscles of Pecten maximus was determined. The calculate dpartial specific volume of 0.74 allowed us to evaluate the molecular weight of the enzyme as 38000.It is concluded that this enzyme consists of a single polypeptide chain on the basis of the molecular weight determined from equilibrium ultracentrifugation in 6 M guanidine hydrochloride and from electrophoresis on polyacrylamide gel containing sodium dodecylsulfate as well as on the basis of the number of peptides obtained by tryptic digestion. The presence of one essential –SH group per mole of enzyme and of one binding site for NADH are also consistent with the existence of a single active center.No NH2‐terminal amino acid can be detected by reaction with dansyl chloride and with phenyl‐isothiocyanate.
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