Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: Cloning and characterization of the coding sequence

被引：45

作者：

Vredendaal, PJCM ^{[1
]}

vandenBerg, IET ^{[1
]}

Malingre, HEM ^{[1
]}

Stroobants, AK ^{[1
]}

Weghuis, DEMO ^{[1
]}

Berger, R ^{[1
]}

机构：

[1] CLIN GENET CTR,3501 CA UTRECHT,NETHERLANDS

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1996年 / 223卷 / 03期

关键词：

D O I：

10.1006/bbrc.1996.0961

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：

The cDNA encompassing the complete coding sequence of human liver short-chain L-3-hydroxyacyl-CoA dehydrogenase (SCHAD) was isolated and characterized. Screening of a cDNA library combined with rapid amplification of 5' cDNA ends resulted in a SCHAD cDNA sequence of 1877 bp. It encodes a protein of 314 amino acids with a calculated molecular weight of 34,3 kDa. containing a mitochondrial import signal peptide of 12 amino acids and 302 amino acids of mature SCHAD protein, The deduced amino acid sequence of the mature protein shows a 92 percent identity with SCHAD from pig heart. Northern blot analysis reveals SCHAD mRNA to be expressed in liver, kidney, pancreas, heart and skeletal muscle. The human SCHAD gene was mapped by fluorescence in situ hybridization to chromosome 4q22-26. (C) 1996 Academic Press, Inc.

引用

页码：718 / 723

页数：6

共 9 条

[1] Mitochondrial short-chain L-3-hydroxyacyl-coenzyme a dehydrogenase deficiency: A new defect of fatty acid oxidation [J].