Nasrin S, Ichinose H, Nagatsu T
Department of Biochemistry, Nagoya University School of Medicine, Japan.
Biochim Biophys Acta. 1992 Feb 1;1118(3):318-22. doi: 10.1016/0167-4838(92)90291-k.
Aromatic L-amino acid decarboxylase (AADC) was purified from bovine adrenal medulla and properties of this enzyme were compared with those of AADC from human pheochromocytoma. The molecular weights of the subunits were identical between human and bovine enzymes and estimated to be 50,000 by SDS-polyacrylamide gel electrophoresis. An isoelectric point of the human enzyme was 5.7, while the bovine enzyme showed several distinct bands at the region of pH 4.9-5.3 in the absence of urea. Multiplicity of the isoelectric point of bovine AADC disappeared in the presence of urea. These results showed that there were some differences between the properties of human and bovine AADC in spite of the high homology (88%) in their primary structures.
从牛肾上腺髓质中纯化出芳香族L-氨基酸脱羧酶（AADC），并将该酶的性质与来自人嗜铬细胞瘤的AADC的性质进行比较。人源和牛源酶亚基的分子量相同，通过SDS-聚丙烯酰胺凝胶电泳估计为50,000。人源酶的等电点为5.7，而在没有尿素的情况下，牛源酶在pH 4.9-5.3区域显示出几条明显的条带。在有尿素存在的情况下，牛AADC等电点的多样性消失。这些结果表明，尽管人源和牛源AADC的一级结构具有高度同源性（88%），但其性质仍存在一些差异。
