The binding of 8-anilinonaphthalene-1-sulphonate to cytoplasmic aspartate aminotransferase from pig heart.
The binding of 8-anilinonaphthalene-1-sulphonate to cytoplasmic aspartate aminotransferase from pig heart.
复制标题
8-苯胺萘-1-磺酸盐与猪心脏细胞质天冬氨酸转氨酶的结合。
DOI：
10.1042/bj1450125
复制
发表时间：
1975
影响因子：
4.1
通讯作者：
P. Bayley
中科院分区：
文献类型：
--
作者：
H. Harris;P. Bayley
苯胺基萘磺酸盐以高亲和力（Kd约10 μ M）和每二聚体一个分子的化学计量学与细胞质天冬氨酸转氨酶结合。它不被脂肪族或芳香族二羧酸酯底物类似物取代。该酶被认为是具有相同亚基的对称二聚体;它可以明显地不对称地结合苯胺基萘磺酸盐。
Anilinonaphthalenesulphonate binds to cytoplasmic aspartate aminotransferase with high affinity (Kd about 10 muM) and with a stoicheiometry of one molecule per dimer. It is not displaced by aliphatic or aromatic dicarboxylate substrate analogues. The enzyme is believed to be a symmetrical dimer with identical subunits; it can evidently function asymmetrically in binding anilinonaphthalenesulphonate.