Solubilization of C18‐Co A and C20‐CoA elongases from Allium porrum L. epidermal cell microsomes

FEBS Letters

Bessoule, Jean-Jacques¹  Cassagne, Claude¹  Lessire, René¹ 

[1]Institut de Biochimie Cellulaire et Neurochimie, CNRS LP 8231,1, Rue Camille Saint-Saëns, 33077 Bordeaux Cedex, France

关键词: Acyl-CoA elongation;    Very long chain fatty acid;    Detergent;    Allium porrum L;    Microsomal enzyme solubilization;    DDT;    dithiothreitol;    VLCFA;    very long chain fatty acids;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(85)81267-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effects of n-octyl-β-D-glucopyranoside, Triton X-100 and deoxycholate on acyl-CoA elongation by Allium porrum L. epidermal cell microsomes showed that the Triton X-100 specifically stimulated the synthesis of C22–C26 acids using C18-CoA as primer, whereas the fatty acid elongation products of C20-CoA remained essentially unchanged. n-Octyl-β-D-glucopyranoside increased the C20 and C22 fatty acid syntheses to the same extent and deoxycholate inhibited C18-CoA and C20-CoA elongation. The presence of two different elongation systems, as suggested by these results, has been demonstrated. After solubilization by Triton X-100, the C18-CoA and C20-CoA elongases were separated by sucrose density centrifugation. The fractions corresponding to sucrose concentrations of 0.51 and 0.62 M presented the maximal activities for C18-CoA and C20-CoA elongases, respectively. In addition, by gel filtration on a Sephacryl S-300 column, the C20-CoA and the C18-CoA elongases have estimated apparent molecular masses under detergent conditions of 600 and 350 kDa, respectively.

【 授权许可】

Unknown