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KMID : 0377619970620030241
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Korean Jungang Medical Journal
1997 Volume.62 No. 3 p.241 ~ p.247
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Study on the Ornithine Aminotransferase in Mouse Small Intestine
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Abstract
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Ornithine aminotransferase(OAT) is known as a mitochondrial enzyme in various tissues including liver and kidney. When enzyme activity in homogenates of small intestine and liver of mouse were compared, small intestine had higher OAT activity per gram tissue than liver. OAT was predominantly localized in cytosolic fraction and not in mitochondrial fraction of small intestine.
The cytosolic OAT of mouse small intestine and mitochondrial OAT of mouse liver were purified to homogeneity using different purification procedures. The purified enzymes showed a single protein band of 46 kDa in SDS-PAGE.
The native molecular weight of cytosolic OAT from mouse small intestine estimated by gel filtration was about 92 kDa that is similar to the mitochondrial OAT of mouse liver. As combining the results of SDS-PAGE and gel filtration, both enzymes might be a dimmer of identical subunits. Some enzymatic properties including substrate specificity, Km values for L-ornithine and a -ketoglutarate, and optimum pH did not show significant differences between cytosolic and mitochondrial OATs.
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