Kinetics of the inactivation of the protein-lipid complex, firefly luciferase, by sodium deoxycholate and its reactivation by phosphatidylcholine

Firely luciferase has been shown to be a protein-lipid complex. Phospholipids and neutral lipids bounds to luciferase have been identified. Sodium deoxycholate rapidly inactivate the enzyme, but an excess of phosphatidylcholine recovered luciferase activity. From the kinetics of inactivation and rea...

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Published inBiochimica et biophysica acta, Protein structure and molecular enzymology Vol. 921; no. 3; pp. 465 - 472
Main Authors Ugarova, N N, Dukhovich, A F, Shvets, S V, Philippova, N Y, Berezin, I V
Format Journal Article
LanguageEnglish
Published 01.01.1987
Subjects
lecithin
Photinus-luciferin 4-monooxygenase (ATP-hydrolysing)
sodium deoxycholate
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Summary:Firely luciferase has been shown to be a protein-lipid complex. Phospholipids and neutral lipids bounds to luciferase have been identified. Sodium deoxycholate rapidly inactivate the enzyme, but an excess of phosphatidylcholine recovered luciferase activity. From the kinetics of inactivation and reactivation, a mechanism for interaction of the enzyme with detergents and phospholipids has been proposed. The substrates ATP and Mg super(2+) stabilized luciferase during delipidation.
Bibliography:ObjectType-Article-1
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ISSN:0167-4838