Partial purification and characterization of alanine racemase from the brackish-water bivalve Corbicula japonica

Alanine racemase from the foot muscle of the brackish-water bivalve Corbicula japonica was partially purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. The molecular weight of the enzyme was estimated as 130000 by gel filtration on Bio-Gel A-1.5m. The pH opti...

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Bibliographic Details
Published in:Journal of experimental marine biology and ecology 1985-12, Vol.94 (1), p.281-289
Main Authors: Omura, Y., Hayashi, Y.S., Matsushima, O., Katayama, H., Yamada, K.
Format: Article
Language:English
Subjects:
alanine racemase
biochemical composition
Biological and medical sciences
bivalve mollusc
brackishwater mollusks
Corbicula japonica
enzymes
Fundamental and applied biological sciences. Psychology
intracellular osmoregulation
Invertebrates
Marine
Mollusca
osmoregulation
Physiology. Development
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Summary:Alanine racemase from the foot muscle of the brackish-water bivalve Corbicula japonica was partially purified by ammonium sulfate fractionation, ion exchange chromatography and gel filtration. The molecular weight of the enzyme was estimated as 130000 by gel filtration on Bio-Gel A-1.5m. The pH optimum was 9.0–9.5 in the l-alanine-to- d-alanine direction and 8.5–9.0 in the d-to- l direction. The apparent K m value for l-alanine was 110 mM and that for d-alanine was 38 mM. Some compounds, which have been known as inhibitors of bacterial alanine racemase, were examined for their inhibitory effects on the bivalve enzyme. Alanine racemase seems to play a significant role in racemization of alanine which is the chief component of the free amino acid pool in relation to intracellular osmoregulation.
ISSN:0022-0981
1879-1697
DOI:10.1016/0022-0981(85)90065-6