MITOCHONDRIAL DOLICHYL-PHOSPHATE MANNOSE SYNTHASE - PURIFICATION AND IMMUNOGOLD LOCALIZATION BY ELECTRON-MICROSCOPY

被引：5

作者：

GASNIER, F ^{[1
]}

ROUSSON, R ^{[1
]}

LERME, F ^{[1
]}

VAGANAY, E ^{[1
]}

LOUISOT, P ^{[1
]}

GATEAUROESCH, O ^{[1
]}

机构：

[1] UNIV LYON 1,LYON S MED SCH,CNRS,INSERM,DEPT BIOCHEM,F-69365 LYONS 2,FRANCE

来源：

EUROPEAN JOURNAL OF BIOCHEMISTRY | 1992年 / 206卷 / 03期

关键词：

D O I：

10.1111/j.1432-1033.1992.tb16993.x

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：

Mitochondrial dolichyl-phosphate mannose synthase has been purified to homogeneity using an original procedure, reconstitution into specific phospholipid vesicles and sedimentation on a sucrose gradient as final step. The enzyme has an apparent molecular mass of 30 kDa on an SDS/polyacrylamide gel. Increased enzyme activity could be correlated with this polypeptide band. A specific antibody was raised in rabbits against this transferase. Specific IgG obtained from the immune serum removed enzymatic activity from a detergent extract of mitochondrial outer membrane and reacted specifically with the 30-kDa band on immunoblots. Furthermore, an immunocytochemical experiment proved the localization of dolichyl-phosphate mannose synthase on the cytosolic face of the outer membrane of mitochondria.

引用

页码：853 / 858

页数：6

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