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J. Biochem, 1976, Vol. 80, No. 1 129-134
© 1976 Japanese Biochemical Society

research-article

Stabilization of Human Serum Alkaline Phosphatase to Histidine-induced Heat Inactivation by Tryptic Digestion

Tatsuhisa YAMASHITA*,1, Etsuko SAWANOBORI-ISOBE* and Matsuhiro MORI**

*Department of Biochemistry, School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113
**Department of Obstetrics and Gynecology, School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113

1. Serum alkaline phosphatase [EC 3.1.3.1 [EC] ] was strongly inactivated by histidine during incubation at pH 8.0 and 45°; however, tryptic digestion of the serum strongly protected the enzyme against inactivation by histidine. In the absence of histidine, however, neither heat inactivation of the phosphatase nor the effect of trypsin [EC 3.4.21.4 [EC] ] was observed. Factors affecting the alkaline phosphatase inactivation were studied further.

2. The effect of trypsin on the histidine-induced heat inactivation differed considerably according to the tissue source of the enzyme, which suggests a possible method for distinguishing alkaline phosphatase isoenzymes.

1 Present address: Laboratory of Physiological Chemistry, School of Medicine, Juntendo University, Bunkyo-ku, Tokyo 113


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