A rotographic study of mutarotase

Abstract

Glucose oxidase is a specific enzyme which catalyses the oxidation (dehydrogenation) of glucose. It was studied in detail during the past fifty years and was proved to be identical with penicillin A, penicillin B and Notatin (see Theorell, 1951). It has been pre- pared in a highly purified form by Coulthard et al. (1945), and its characteristics have been firmly established by Keilin & Hartree (1948a). Its specificity is truly remarkable, as shown by these authors (Keilin & Hartree, 1952 a), in that essentially only ,8-D-glucose is oxidized by the enzyme. In the course of these studies, they noted certain irregularities and they concluded that some glucose oxidase preparations contained another agent, which they called mutarotase. This was in accord- ance with an earlier observation by Keilin & Hartree (1952b) indi- cated, in their succeeding paper, that this agent is a different entity from glucose oxidase and it is probably an enzyme which catalyses the mutarota- tion of glucose. Based on the molecular weight deternination of as comparedto the best inorganic catalyst, namely the hydroxyl ion, with a coefficient of 8.8 x 103 min.-. For this