SOLUBILIZATION OF MEMBRANE-BOUND DELTA(12)-FATTY-ACID AND DELTA(6)-FATTY-ACID DESATURASES FROM BORAGE SEEDS

Citation
Am. Galle et al., SOLUBILIZATION OF MEMBRANE-BOUND DELTA(12)-FATTY-ACID AND DELTA(6)-FATTY-ACID DESATURASES FROM BORAGE SEEDS, Phytochemistry, 45(8), 1997, pp. 1587-1590
Citations number
35
Categorie Soggetti
Plant Sciences
Journal title
ISSN journal
00319422
Volume
45
Issue
8
Year of publication
1997
Pages
1587 - 1590
Database
ISI
SICI code
0031-9422(1997)45:8<1587:SOMDAD>2.0.ZU;2-J
Abstract
Solubilization of two membrane-bound enzymes (Delta(12)- and Delta(6)- desaturases) involved in the biosynthesis of polyunsaturated fatty aci ds (linoleic 18:2 and gamma-linolenic acids gamma-18:3, respectively) was performed using borage seed microsomes. Of the three detergents Tr iton X100, sodium deoxycholate and CHAPS, the latter was found to be t he most efficient for solubilization and maintaining the two desaturas e activities. Solubilization was optimal with 1% CHAPS at a detergent- membrane protein ratio equal to one. Under these conditions, only 55% of the microsomal proteins were solubilized. These results are promisi ng for further purification of the two desaturases. (C) 1997 Elsevier Science Ltd. All rights reserved.