Noguchi T, Okuno E, Kido R
Biochem J. 1977 Jan 1;161(1):177-9. doi: 10.1042/bj1610177.
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.
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。
