MOLECULAR-CLONING AND FUNCTIONAL EXPRESSION OF A HUMAN PEROXISOMAL ACYL-COENZYME-A OXIDASE

被引:35
|
作者
AOYAMA, T
TSUSHIMA, K
SOURI, M
KAMIJO, T
SUZUKI, Y
SHIMOZAWA, N
ORII, T
HASHIMOTO, T
机构
[1] SHINSHU UNIV,SCH MED,DEPT PEDIAT,MATSUMOTO,NAGANO 390,JAPAN
[2] GIFU UNIV,SCH MED,DEPT PEDIAT,GIFU 500,JAPAN
关键词
D O I
10.1006/bbrc.1994.1158
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
cDNA encoding the human peroxisomal acyl-coenzyme A oxidase (AOX) was cloned and sequenced. The longest cDNA insert isolated has 3083 bases and encodes the entire protein of 661-amino acids, including the carboxyl-terminal sequence (Ser-Lys-Leu) known as a minimal peroxisome-targeting signal. At the amino acid level, the significantly high homology (89%) to rat AOX was found. In the cDNA-expression experiment, significant amount of AOX was accumulated in human skin fibroblast and the expressed AOX was catalytically active, while only a limited amount was found in Zellweger syndrome patient’s fibroblast not having normal peroxisomes. © 1994 Academic Press, Inc.
引用
收藏
页码:1113 / 1118
页数:6
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