PMID: 2492796Jan 1, 1989

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

Archives of Microbiology
M PriyolkarD 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.

Citations

Oct 15, 1979·European Journal of Biochemistry·F Widmer, J L Leuba
Oct 1, 1977·Journal of Bacteriology·B G Hall, E C Reeve
Jul 1, 1976·Applied and Environmental Microbiology·J D Efstathiou, L L McKay
Aug 1, 1973·Journal of General Microbiology·P A Fantes, C F Roberts
May 1, 1972·Journal of Bacteriology·J T UlrichK L Temple
Jun 1, 1968·Journal of Bacteriology·M L MorseW Hengstenberg
Mar 1, 1966·Analytical Biochemistry·M Messer, A Dahlqvist
May 1, 1981·Biokhimii︠a︡·E V LetunovaA Ia Khorlin
Apr 1, 1965·Journal of Bacteriology·J E CITTIP R ELLIKER
Apr 1, 1981·Applied and Environmental Microbiology·B J Macris, P Markakis
Nov 1, 1981·Applied and Environmental Microbiology·R J Snook, L L McKay

Related Concepts

Sephadex G 200
Anhydrous lactose
Corynebacterium
Galactose Measurement
GLB1
Chromatography
Galactose
DEAE-Sephadex A-50
Enzyme agent
DEAE-Cellulose

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