[Beta-cyanoalanine synthase: Its purification and basic physico-chemical properties].
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.
D000596:Amino Acids / Q000032:analysis; D013437:Carbon-Sulfur Lyases / Q000032:analysis* / Q000302:isolation & purification; D005591:Chemical Fractionation; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004589:Electrophoresis, Disc; D004591:Electrophoresis, Polyacrylamide Gel; D008190:Lyases / Q000032:analysis*; D008928:Mitochondria / Q000201:enzymology; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D011730:Pyridoxal / Q000032:analysis
D000596:Amino Acids; D011730:Pyridoxal; D008190:Lyases; D013437:Carbon-Sulfur Lyases
Beta-tsianoalaninsintaza: Ochistka i osnovnye fiziko-khimicheskie svoĭstva