Priyolkar M, Nair C K, Pradhan D S
Biochemistry Division, Bhabha Atomic Research Centre, Trombay, Bombay, India.
Arch Microbiol. 1989;151(1):49-53. doi: 10.1007/BF00444668.
The beta-galactosidase (EC 3.2.1.32) of Corynebacterium murisepticum (inducible by lactose and galactose) was purified by successive column chromatography on Sephadex G-200, DEAE-Sephadex A-50 and DEAE-cellulose (DE52). The enzyme was found to be a dimer of identical subunits of molecular mass 100,000 daltons. The Km values of the enzyme for the substrates lactose and o-nitrophenyl-beta-D-galactopyranoside (ONPG) are 16.7 mM and 4.4 mM, respectively, indicating, its low affinity for the substrates. The Ouchterlony immunodiffusion method exhibited immunological homogeneity of the enzyme preparation. The catalytic site of the enzyme does not take part in antigen-antibody reaction.
鼠败血棒状杆菌的β-半乳糖苷酶（EC 3.2.1.32，可被乳糖和半乳糖诱导）通过在葡聚糖凝胶G-200、二乙氨基乙基葡聚糖A-50和二乙氨基乙基纤维素（DE52）上连续进行柱色谱法进行纯化。该酶被发现是由分子量为100,000道尔顿的相同亚基组成的二聚体。该酶对底物乳糖和邻硝基苯基-β-D-吡喃半乳糖苷（ONPG）的Km值分别为16.7 mM和4.4 mM，表明其对底物的亲和力较低。双向免疫扩散法显示该酶制剂具有免疫同质性。该酶的催化位点不参与抗原-抗体反应。
