Rapid purification and characterization of cystine lyase b from broccoli inflorescence

Authors
Citation
K. Ukai et J. Sekiya, Rapid purification and characterization of cystine lyase b from broccoli inflorescence, PHYTOCHEM, 51(7), 1999, pp. 853-859
Citations number
27
Categorie Soggetti
Agricultural Chemistry","Animal & Plant Sciences
Journal title
PHYTOCHEMISTRY
ISSN journal
00319422 → ACNP
Volume
51
Issue
7
Year of publication
1999
Pages
853 - 859
Database
ISI
SICI code
0031-9422(199908)51:7<853:RPACOC>2.0.ZU;2-8
Abstract
We found three isoforms (a, b, and c) of cystine lyase in broccoli (Brassic a oleracea var. italica) inflorescence tissues. Cystine lyase b, the most a bundant isoform, was rapidly purified to homogeneity. The native enzyme had a M-r. of 160,000 and composed of four identical subunits with a M-r of 40 ,000. Thiocysteine and pyruvate were confirmed as reaction products. The pu rified cystine lyase b utilized L-cystine and S-alkyl L-cysteine sulfoxide as substrates. Other properties of cystine lyase b were almost similar to t hose of the isoform a as reported previously. Cystine lyase a and b were lo calized in cytosolic and/or vacuole fraction. A high activity of cystine ly ase was detected in some Allium species in addition to Cruciferae plants. ( C) 1999 Elsevier Science Ltd. All rights reserved.