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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 18, Number 6
BKCSDE 18(6)
June 20, 1997 

Purification and Characterization of the Recombinant Arabidopsis thaliana Acetolactate Synthase
Kyubong Jo, Seongtaek Hong, Myung-Un Choi, Soo-Ik Chang, Jung-Do Choi, Eun-Hie Koh
Acetolactate synthase was purified from Escherichia coli MF2000/pTATX containing Arabidopsis thaliana acetolactate synthase gene. Purification steps included DEAE cellulose ion exchange column chromatography, phenyl sepharose hydrophobic column chromatography, hydroxylapatite affinity column chromatography, and Mono-Q HPLC. Molecular weight was estimated to be ∼65 KDa and purification fold was 109 times. The enzyme showed a pH optimum of 7 and the KM value was 5.9 mM. The purified enzyme was not inhibited by any of the end products, valine, leucine, and isoleucine.
648 - 653
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