PMID: 6404304Feb 15, 1983Paper

Catalytic properties of Sepharose-bound L-alanine dehydrogenase from Bacillus cereus

Biochimica Et Biophysica Acta
L MureşanO Bârzu

Abstract

(1) L-Alanine dehydrogenase from Bacillus cereus was purified by a two-step chromatographic procedure involving Cibacron-Blue 3G-A Sepharose 4B-CL, and Sepharose 6B-CL, and immobilized on CNBr-activated Sepharose 4B. (2) Following immobilization via two of the six subunits, L-alanine dehydrogenase retained 66% of the specific activity of the soluble enzyme. The affinity of the immobilized enzyme for NH4+, pyruvate and L-alanine, was not different to that of the soluble form. The Km of the Sepharose-bound L-alanine dehydrogenase for pyridine coenzymes was 6-8-times higher than in the soluble case. (3) The stability of L-alanine dehydrogenase towards urea or thermal denaturation was increased by immobilization. (4) The incubation at 37 degrees C for 24 h of the immobilized L-alanine dehydrogenase with 3 M NH4Cl/NH4OH buffer (pH 9) released 70% of the enzyme. The specific activity and the affinity of the 'solubilized' L-alanine dehydrogenase for the pyridine coenzymes was the same as that obtained with the original, soluble L-alanine dehydrogenase.

References

Oct 1, 1979·European Journal of Biochemistry·T Ohashima, K Soda
May 1, 1976·FEBS Letters·G F Bickerstaff, N C Price
Dec 17, 1973·European Journal of Biochemistry·W W ChanK Brand
Jan 1, 1974·Methods in Enzymology·T Kristiansen
Jun 28, 1972·Journal of Chromatography·H J BöhmeE Hofmann
Jan 1, 1974·Journal of Biomedical Materials Research·P H NewellB K Chakraborty
Dec 9, 1970·Biochemical and Biophysical Research Communications·W W Chan
Sep 9, 1980·Biochimica Et Biophysica Acta·Z VáliP Závodszky
Jan 1, 1964·Journal of Bacteriology·N G MCCORMICK, H O HALVORSON

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