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J. Biochem, 1984, Vol. 95, No. 6 1811-1818
© 1984 Japanese Biochemical Society

research-article

Purification and Some Properties of Bovine Liver Cytosol Thioltransferase

Mitsuhiro HATAKEYAMA, YORIKO TANIMOTO and Tadashi MIZOGUCHI

Laboratory of Biochemistry, Faculty of Pharmaceutical Sciences, Osaka University Suita, Osaka 565

A cytosol thioltransferase was purified 37,000-fold from bovine liver by essentially the same procedure as reported for rat liver enzyme by Axelsson et al. ((1978) Biochemistry 17, 2978–2984). The purified enzyme appears to be homogeneous on sodium dodecyl sulfate (SDS)-gel electrophoresis and has a molecular weight (Mr) of 11,000, an isoelectric point (pI) of 8.1, and an optimum pH with S-sulfocysteine and GSH as substrates of 8.5. It is specific for disulfides including L-cystine, S sulfocysteine, ribonuclease A, trypsin, soybean Kunitz trypsin inhibitor, soybean Bowman Birk trypsin inhibitor and insulin, and converts Bowman Birk trypsin inhibitor to an inactive form.

The enzyme does not act as a protein : disulfide isomerase, as measured by reactivation of "scramble" ribonuclease and Kunitz soybean trypsin inhibitor. Thioltransferase activity was found in cytosol of various bovine tissues.


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