Affinity purification, crystallization, and amino acid analysis of hog kidney mutarotase type II.

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Hog kidney mutarotase type II was purified to polyacrylamide disc gel electrophoretic homogeneity by a five-step procedure including affinity chromatography with phloretin-linked agarose. The purified enzyme was crystallized, and the crystals were subjected to amino acid analysis. The amino acid composition of the enzyme was similar to that of bovine kidney mutarotase, except for marked differences in the contents of phenylalanine and methionine.

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