Purification and properties of hog kidney mutarotase.

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Abstract
Hog kidney mutarotase was separated into 4 forms (types I-IV) by DEAE-cellulose column chromatography. The most abundant form (type II) was purified to homogeneity as judged by polyacrylamide disc gel electrophoresis. The physico-chemical properties of the pure type II enzyme were as follows: MW, 41,000; isoelectric point, pH 5.48; Km for .alpha.-D-glucose at pH 7.4 and at 25.degree., 19 mM; optimum pH 6.5-7.5; optimum temperature, 30.degree.. The enzyme activity was greatly reduced at acid pH below 6.0. The enzyme lost little activity on storage for at least 130 days at 4.degree., about 12% of the activity was lost during the same period at -20.degree.. When the enzyme was heated for 10 min at 59.degree., the activity was completely lost.

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