LIPID-BINDING PROPERTIES OF A FACTOR NECESSARY FOR LINOLEIC-ACID DESATURATION

被引：17

作者：

LEIKIN, AI

NERVI, AM

BRENNER, RR

机构：

[1] Instituto de Fisiología, Cátedra de Bioquímica, Facultad de Ciencias Médicas, Universidad Nacional de La Plata, Plata, 1900 La

来源：

LIPIDS | 1979年 / 14卷 / 12期

关键词：

D O I：

10.1007/BF02533440

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Suspension and centrifugation of crude microsomes of rat liver in low ionic strength solution separated a soluble protein fraction that is necessary for the full activity of the linoleic acid desaturase. The fraction partially purified through Sephadex G-150 still retains lipids which are mainly constituted by phosphatidylcholine. Linoleic acid predominates in the fatty acid composition. By NaCl gradient centrifugation and electrophoresis in gelatinized cellulose acetate, the factor behaves like a lipoprotein. The factor binds linoleic acid and linolyl-CoA that are desaturated to γ-linolenic acid when incubated with washed microsomes. Albumin does not replace the factor. © 1979 American Oil Chemists' Society.

引用

页码：1021 / 1026

页数：6

共 18 条

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