人心肌线粒体天冬氨酸氨基转移酶的一级结构。
The primary structure of mitochondrial aspartate aminotransferase from human heart.
作者信息
Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F
出版信息
Biochim Biophys Acta. 1985 Nov 8;832(1):46-51. doi: 10.1016/0167-4838(85)90172-4.
The complete amino acid sequence of the mitochondrial aspartate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from human heart has been determined based mainly on analysis of peptides obtained by digestion with trypsin and by chemical cleavage with cyanogen bromide. Comparison of the sequence with those of the isotopic isoenzymes from pig, rat and chicken showed 27, 29 and 55 differences, respectively, out of a total of 401 amino acid residues. Evidence for structural microheterogeneity at position 317 has also been obtained.
人心脏线粒体天冬氨酸氨基转移酶（L-天冬氨酸：2-氧代戊二酸氨基转移酶，EC 2.6.1.1）的完整氨基酸序列主要是通过对用胰蛋白酶消化和用溴化氰化学裂解得到的肽段进行分析来确定的。将该序列与猪、大鼠和鸡的同工酶序列进行比较，在总共401个氨基酸残基中分别发现了27个、29个和55个差异。还获得了第317位存在结构微异质性的证据。
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