MOLECULAR-CLONING AND AMINO-ACID-SEQUENCE OF THE PORCINE 17-BETA-ESTRADIOL DEHYDROGENASE

被引:92
作者
LEENDERS, F [1 ]
ADAMSKI, J [1 ]
HUSEN, B [1 ]
THOLE, HH [1 ]
JUNGBLUT, PW [1 ]
机构
[1] MAX PLANCK INST EXPTL ENDOCRINOL,D-30603 HANNOVER,GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1994年 / 222卷 / 01期
关键词
D O I
10.1111/j.1432-1033.1994.tb18860.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
We describe the cloning and sequencing of porcine 17 beta-estradiol dehydrogenase. The enzyme performs oxidation 360-fold more efficiently than reduction, both measured under optimal conditions. It is localized in specialized vesicles of epithelial cells. The cDNA clones were isolated from a lambda UNI ZAP XR library of porcine kidney and polymerase-chain-reaction-amplified from templates of uterus epithelium. In both tissues, the same enzyme is coded by a transcript of 2.9 kb. It contains a 69-b 5'-noncoding region, an open reading frame of 2211 b and a 3'-noncoding region of 624 b. The open reading frame of 737 amino acids with a predicted molecular mass 79973Da was confirmed by amino acid sequencing of peptides. The 80-kDa translation product is processed to the N-terminal 32-kDa enzyme, part of which is then covalently linked to actin. The estradiol dehydrogenase/actin complex and the 80-kDa translation product comigrate in SDS/PAGE.
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页码:221 / 227
页数:7
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