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KMID : 0377219810060010261
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Medical Journal of Chosun Univercity
1981 Volume.6 No. 1 p.261 ~ p.268
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Studies on the Regulating Mechanism of Gamma-Glutamyl Transpeptidase Activity in Rats
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Cha Jong-Hee
Park Jae-Yoon
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Abstract
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Gamma-glutamyl transpeptidase, a membrane-bound enzyme, is Known to be inhibited by L-serine particulary in sodium borate buffer. we studied the regulating mechanism of gamma-glutamyl transpeptidase activity by phenobarbital, ethanol, phosphatidycholine and phosphatidylethanolamine. Phenobarbital and ethanol elevated the activity of gamma-glutamyl transpeptidase with similar stimulatory pattern at microsomal level due to the microsomal of rats. And these stimulatory effects might be due to the microaomal injury and cytoplasmic infiltration. Phosphatidylcholine and phosphatidylethanolamine inhibited the activity of gamma-glutamyl transpeptidase with similar inhibitory pattern in liver and serum of rats. It might be due to the change of sensitivity of gamma-glutamyl transpeptidase as a membranebound enzyme by phospholipids and the decreased solubility of substrate. Phosphatidylaholine and phosphatidylethanolamine were found to be the two ’quantitatively dominating phosphatidyl derivatives of tissues, making up about 3/4 of total phospholipids. Phosphatidylcholine and phosphatidylethanolamine may serve as substrate for the incorporation of L-serine and ethanolamine into microsome.
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KEYWORD
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Gamma-Glutamyl transpeptidase
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