PMID: 2492796Jan 1, 1989

Purification and characterisation of an inducible beta-galactosidase from Corynebacterium murisepticum

Archives of Microbiology
M PriyolkarD S Pradhan


The beta-galactosidase (EC 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.


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Related Concepts

Sephadex G 200
Anhydrous lactose
Galactose Measurement
DEAE-Sephadex A-50
Enzyme agent

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