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J. Biochem, 1982, Vol. 91, No. 6 1889-1898
© 1982 Japanese Biochemical Society

research-article

Purification and Characterization of Multiple Forms of Mutarotase from Hog Kidney Cortex1

Yukiyasu TOYODA, Ichitomo MIWA and Jun OKUDA

Department of Clinical Biochemistry, Faculty of Pharmacy, Meijo University Tempaku-ku, Nagoya, Aichi 468

The enzyme mutarotase [aldose 1-epimerase, EC 5.1.3.3 [EC] ] from hog kidney cortex was separated into four fractions (designated types I, II,III, and IV in order of elution) by column chromatography on DEAE-ellulose. Two major forms, types I and II, were purified to homogeneity as judged by polyacrylamide gel electropho-resis and isoelectric focusing on thin layer polyacrylamide gel.

Types I, II, III, and IV had isoelectric points of 5.78, 5.48, 5.23, and 5.10, respectively. The following physicochemical properties were common to all four types: molecular weight, 41,000; Km for {alpha}-D-glucose at pH 7.4 and 25°C, 19mM; optimum pH, 6.5–7.5; optimum temperature, 3O-37°C; heat stability, up to 50°C.

On double immunodiffusion, the four types of mutarotase gave single precipitin lines, which fused completely with each other, against the antibody to purified type II enzyme.

Types I and II had an identical amino-terminal residue, arginine, and an identical carboxyl-terminal sequence, -(Phe-Phe-Ser-Val)-Val-Ala. The amino acid composition of type I was almost identical with that of type II. Very similar tryptic peptide maps were obtained from types I and II, with only a few points of variance.

1This study was supported in part by Science Research Grants from the Ministry of Education, Science and Culture of Japan.


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