Abstract
Solubilization of two membrane-bound enzymes (Δ 12- and Δ 6-desaturases) involved in the biosynthesis of polyunsaturated fatty acids (linoleic 18:2 and γ-linolenic acids γ-18:3, respectively) was performed using borage seed microsomes. Of the three detergents Triton X100, sodium deoxycholate and CHAPS, the latter was found to be the most efficient for solubilization and maintaining the two desaturase 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 promising for further purification of the two desaturases. © 1997 Elsevier Science Ltd. All rights reserved
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