Hongo S, Ito H, Takeda M, Sato T
Enzyme. 1986;36(4):232-8. doi: 10.1159/000469299.
Identification of rat liver mitochondrial asparagine-pyruvate transaminase with phenylalanine-pyruvate transaminase has been done. When a mitochondria extract was subjected to isoelectric focusing, the two enzyme activities were identically focused. This procedure and DEAE-Sepharose chromatography revealed multiple forms of the enzyme, in which the main form was purified. In the various purification steps the two enzyme activities appeared in the same fraction. The enzyme of the final preparation step gave a single band in polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate. During the purification, a similar increase of the specific activity and yield were obtained in the two activities. Phenylalanine was found to be a competitive inhibitor of asparagine transaminase. These results suggest the identity of the two enzymes.
已完成大鼠肝脏线粒体天冬酰胺 - 丙酮酸转氨酶与苯丙氨酸 - 丙酮酸转氨酶的鉴定。当线粒体提取物进行等电聚焦时，这两种酶活性聚焦于同一位置。此方法以及二乙氨基乙基 - 琼脂糖凝胶柱色谱法揭示了该酶的多种形式，其中主要形式已被纯化。在各个纯化步骤中，这两种酶活性出现在同一组分中。最终制备步骤的酶在有和没有十二烷基硫酸钠存在的情况下，在聚丙烯酰胺凝胶电泳中均呈现单一条带。在纯化过程中，这两种活性的比活性和产率都有类似的增加。发现苯丙氨酸是天冬酰胺转氨酶的竞争性抑制剂。这些结果表明这两种酶是相同的。
