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7 hasil
Cleavage of L-cystine by soluble enzyme preparations from Brassica species.
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Enzymatic degradation of L-cystine by cytoplasmic particles from cabbage leaves.
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The C-S Lyases of Higher Plants : Isolation and Properties of Homogeneous Cystine Lyase from Broccoli (Brassica oleracea var botrytis) Buds.
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Cystine lyase degrades l-cystine by a beta-elimination to form cysteine persulfide, pyruvate, and ammonia. This enzyme is common in Brassica sp. and has been purified to homogeneity from extracts of broccoli (Brassica oleracea var botrytis) buds. Two isozymes were separated on DEAE-Fractogel columns
Biochemical characterization of cystine lyase from broccoli (Brassica oleracea var. italica).
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Cystine lyase is the enzyme responsible for off-aroma deterioration in fresh unblanched broccoli. In this research, cystine lyase purification from broccoli has been optimized. Only one protein peak with cystine lyase activity was found during purification. Broccoli cystine lyase was purified
Purification and Characterization of Cystine Lyase a from Broccoli Inflorescence.
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One of the three isoforms of an enzyme degrading L-cystine was purified to homogeneity from broccoli (Brassica oleracea var. italica) inflorescences, with use of a sensitive assay based on derivatization of a reaction product with monobromobimane. The reaction product with a thiol group was found to
A new member of plant CS-lyases. A cystine lyase from Arabidopsis thaliana.
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Cystine lyases catalyze the breakdown of l-cystine to thiocysteine, pyruvate, and ammonia. Until now there are no reports of the identification of a plant cystine lyase at a molecular level, and it is not clear what biological role this class of enzymes have in plants. A cystine lyase was isolated
Partial Purification and Characterization of Cystine Lyase from Cabbage (Brassica oleracea var capitata).
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Cabbage (Brassica oleracea var capitata) leaves were used as a source of cystine lyase. Diethylaminoethyl-cellulose chromatography resolved two peaks of activity, designated I and II.Cystine lyase I (molecular weight 145,000) and O-acetylserine sulfhydrylase (molecular weight 70,000) were resolved
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