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The localization, partial purification and regulation of pea plastid HMG-CoA reductase.

Abstract：

:HMG-CoA reductase was located to the envelope membranes of pea etioplasts, the first report of the suborganelle localization of this key enzyme in isoprenoid synthesis. The enzyme was purified 156 fold from isolated envelope membranes. Purification was achieved by detergent solubilization, hydroxylapatite chromatography and glycerol gradient centrifugation. Membrane-bound etioplast HMG-CoA reductase was activated 4 to 5 fold by high concentrations of inorganic phosphate, this activation was prevented by arsenate, a structural analog of phosphate.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Wilson TM,Russell DW

doi

10.1016/0006-291x(92)91227-h

subject

Has Abstract

pub_date

1992-04-15 00:00:00

pages

530-7

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(92)91227-H

journal_volume

184

pub_type

杂志文章

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