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- W2028733316 abstract "Various procedures for the preparation of protein fractions from onion, capable of converting S-alkyl-l-cysteine sulfoxides to ammonia, pyruvate, and alkyl alkane thiosulfinates are described. The identity of alliinase-produced carbonyl as pyruvic acid was established by the infrared spectrum of its 2,4-dinitrophenylhydrazone and by coupling alliinase action to lactic dehydrogenase via reduced diphosphopyridine nucleotide. The enzyme acted maximally in the presence of pyridoxal phosphate and pyrophosphate buffer at pH 8.5–8.8, is very unstable at acid pH's, and possesses a Km of about 4 × 10−3M with (±)) S-propyl-l-cysteine sulfoxide as substrate. Evidence is presented for the role of pyridoxal phosphate as coenzyme of alliinase. The presence of the l-cysteine moiety and the sulfoxide grouping are absolute requirements for substrate specificity. The dextrarotatory diastereomers of the S-substituted l-cystine sulfoxides were hydrolyzed more rapidly than were the corresponding levorotatory forms. The unresolved S-propyl derivative was hydrolyzed faster than were both the S-methyl and most synthetic preparations of S-allyl derivatives employed. A quantitative method for the determination of thiolsulfinates is presented." @default.
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- W2028733316 date "1963-01-01" @default.
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- W2028733316 title "Characterization of alliinase of Allium cepa (onion)" @default.
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- W2028733316 doi "https://doi.org/10.1016/0003-9861(63)90035-3" @default.
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