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KMID : 0357919810150020119
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Korean Journal of Pathology
1981 Volume.15 No. 2 p.119 ~ p.123
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Study on Ornithine Amininotransferase from Human Tissues
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송만수<지도김형로교수>/Man Soo Song
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Abstract
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The properties of ornithine aminotransferase, which catalyzes the transfer of
S-NH2 group of ornithine to α-ketoacids were characterized in the
post-mortem human tissues. The enzyme was distributed in all human tissues tested
especially high in small intestine and its activity was increasing in liver and kindey but
decreasing in small intestine with age.
The intestinal enzyme being reactive with α-ketoglutarate, glyoxylate, pyruvate and
oxaloacetate in decreasing order was very heat-unstable but its inactivation ty
heat-treatment was partially prevented by the presence of pyridoxal phosphate.
The enzyme was completely inhibited by p-hydroxy-mercuritenzoate, suggesting that
SH-group of enzyme protein is essential for catalytic action.
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KEYWORD
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