Belen'kiĭ D M, Mikhaĭlov V I, Shaptseva V N
Biokhimiia. 1982 Jul;47(7):1141-6.
Chemical modification of the COOH-groups of acid alpha-glucosidase from human liver by 1-ethyl-3 (3'-dimethylaminopropyl) carbodiimide. HCl in the presence of rho-aminophenyl-beta-D-galactopyranoside was carried out. The presence of covalently bound galactose derivative in the enzyme was followed by changes in the absorption spectra and electrophoretic mobility during polyacrylamide gel electrophoresis and by the ability of modified alpha-glucosidase to interact specifically with castor-bean lectin (RCA II). The modified enzyme retained its catalytic activity towards maltose and did not differ from native alpha-glucosidase in terms of its affinity for this substrate, the Km values for maltose during 5 and 6 mM, respectively. The in vitro changes in the marker specificity of acid alpha-glucosidase against the unchanged catalytic properties of the enzyme are discussed.
在对氨基苯基-β-D-吡喃半乳糖苷存在的情况下，用1-乙基-3-(3'-二甲氨基丙基)碳二亚胺盐酸盐对人肝脏酸性α-葡萄糖苷酶的羧基进行化学修饰。通过聚丙烯酰胺凝胶电泳过程中吸收光谱和电泳迁移率的变化，以及修饰后的α-葡萄糖苷酶与蓖麻凝集素（RCA II）特异性相互作用的能力，追踪酶中共价结合的半乳糖衍生物的存在情况。修饰后的酶保留了对麦芽糖的催化活性，并且在对该底物的亲和力方面与天然α-葡萄糖苷酶没有差异，麦芽糖的Km值分别为5 mM和6 mM。讨论了酸性α-葡萄糖苷酶标记特异性的体外变化与酶催化特性不变之间的关系。
