May 1, 1976

Beta-cyanoalanine synthase: Its purification and basic physico-chemical properties

Biokhimii︠a︡
T N Akopian, E V Goriachenkova

Abstract

A method has been developed for the purification of beta-cyano-L-alanine synthase from etiolated 10-day-old seedlings of blue lupine. High purity preparations of the enzyme were obtained with specific activity exceeding 4000-fold that of the seedling homogenate. Preparations were homogeneous on electrophoresis in polyacrylamide gel. The yield of total activity after purification was approximately 20%. Glutamic acid is the enzyme's only N-terminal amino acid; the molecular weight of the enzyme (both native and treated with 6 M urea) is 52000. The synthase containes one mole of pyridoxal-P per mole of protein; its isoelectric point is situated at pH 4,8. The enzyme's absorption spectrum has a maximum at 410 nm i.e., in the characteristic range of many pyridoxal-U-containing enzymes. Data on the amino acid composition of the enzyme are presented.

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Mentioned in this Paper

Nevus
Polyacrylamide Gels
Enzymes, antithrombotic
Talpidae
SDS-PAGE
Desmolases
Properdin Deficiency, X-LINKED
Chromatography, DEAE-Cellulose
Pyridoxal Phosphate
Hydatidiform Mole

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