PURIFICATION AND CHARACTERIZATION OF THE RECOMBINANT ARABIDOPSIS-THALIANA ACETOLACTATE SYNTHASE

Authors
JO K HONG S CHOI MU CHANG SI CHOI JD KOH EH
Citation
K. Jo et al., PURIFICATION AND CHARACTERIZATION OF THE RECOMBINANT ARABIDOPSIS-THALIANA ACETOLACTATE SYNTHASE, Bulletin of the Korean Chemical Society, 18(6), 1997, pp. 648-653
Citations number
40
Categorie Soggetti
Chemistry
Journal title
Bulletin of the Korean Chemical Society → ACNP
ISSN journal
02532964
Volume
18
Issue
6
Year of publication
1997
Pages
648 - 653
Database
ISI
SICI code
0253-2964(1997)18:6<648:PACOTR>2.0.ZU;2-S
Abstract
Acetolactate synthase was purified from Escherichia coli MF2000/pTATX containing Arabidopsis thaliana acetolactate synthase gene. Purificati on steps included DEAE cellulose ion exchange column chromatography, p henyl sepharose hydrophobic column chromatography, hydroxylapatite aff inity column chromatography, and Mono-Q HPLC. Molecular weight was est imated to be similar to 65 KDa and purification fold was 109 times. Th e enzyme showed a pH optimum of 7 and the K-M value was 5.9 mM. The pu rified enzyme was not inhibited by any of the end products, valine, le ucine, and isoleucine.