Abstract
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.
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