| Literature DB >> 2492796 |
M Priyolkar1, C K Nair, D S Pradhan.
Abstract
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.Entities:
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Year: 1989 PMID: 2492796 DOI: 10.1007/bf00444668
Source DB: PubMed Journal: Arch Microbiol ISSN: 0302-8933 Impact factor: 2.552