大鼠肾组氨酸-丙酮酸氨基转移酶与谷氨酰胺-氧代酸氨基转移酶的同一性。
Identity of rat kidney histidine-pyruvate aminotransferase with glutamine-oxo acid aminotransferase.
作者信息
Noguchi T, Okuno E, Kido R
出版信息
Biochem J. 1977 Jan 1;161(1):177-9. doi: 10.1042/bj1610177.
Abstract
Histidine-pyruvate aminotransferase and glutamine-phenylpyruvate aminotransferase were purified from rat kidney by the same procedure. The ratio of the two activities remained constant during purification and was unchanged by a variety of treatments of the purified enzyme. Glutamine was found to act as a competitive inhibitor of histidine-pyruvate aminotransferase. These results suggest that rat kidney histidine-pyruvate aminotransferase is identical with glutamine-oxo acid aminotransferase. Identity of the two enzymes in other tissues of rats is discussed.
摘要
通过相同的程序从大鼠肾脏中纯化出组氨酸-丙酮酸转氨酶和谷氨酰胺-苯丙酮酸转氨酶。在纯化过程中，这两种酶活性的比例保持恒定，并且对纯化后的酶进行各种处理后该比例也未发生变化。发现谷氨酰胺可作为组氨酸-丙酮酸转氨酶的竞争性抑制剂。这些结果表明，大鼠肾脏中的组氨酸-丙酮酸转氨酶与谷氨酰胺-氧代酸转氨酶是相同的。本文还讨论了这两种酶在大鼠其他组织中的同一性。
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本文引用的文献
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2
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3
Assays of glutamine and its aminotransferase with the enol-borate of phenylpyruvate.用苯丙酮酸烯醇硼酸酯对谷氨酰胺及其转氨酶进行测定。
Arch Biochem Biophys. 1970 Jan;136(1):178-86. doi: 10.1016/0003-9861(70)90339-5.
4
Purification, characterization and identification of rat liver histidine-pyruvate aminotransferase isoenzymes.大鼠肝脏组氨酸-丙酮酸转氨酶同工酶的纯化、表征及鉴定
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6
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