Yagi T, Misono H, Kurihara N, Yamamoto T, Soda K
J Biochem. 1980 May;87(5):1395-402. doi: 10.1093/oxfordjournals.jbchem.a132880.
L-Lysine:2-oxoglutarate 6-aminotransferase from Flavobacterium lutescence (= Achromobacter liquidum) has been shown to be composed of one each of four non-identical subunits, A, B1, B2, and C. The subunits were isolated by gel filtration, and DEAE-cellulose chromatography in the presence of 8 M urea. Their molecular weights were determined by ultracentrifugation, gel electrophoresis and gel filtration: subunit A 24,000; B1 28,000; B2 28,000; C 45,000. These subunits were all different in amino acid composition. Of the two molecules of bound pyridoxal 5'-phosphate, the one which absorbs at 415 nm is bound to subunit B2 and participates in the catalytic action of the enzyme.
来自黄色黄杆菌(= 液化无色杆菌)的L-赖氨酸:2-氧代戊二酸6-氨基转移酶已被证明由四个不同亚基A、B1、B2和C各一个组成。这些亚基通过凝胶过滤和在8M尿素存在下的DEAE-纤维素色谱法分离。通过超速离心、凝胶电泳和凝胶过滤测定它们的分子量:亚基A为24,000;B1为28,000;B2为28,000;C为45,000。这些亚基的氨基酸组成均不同。在两个结合的磷酸吡哆醛分子中,在415nm处有吸收的那个与亚基B2结合并参与酶的催化作用。