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Molecular cloning, cDNA structure and predicted amino acid sequence of bovine 3β‐hydroxy‐5‐ene steroid dehydrogenase/Δ 5 ‐Δ 4 isomerase
Author(s) -
Zhao Hui-Fen,
Simard Jacques,
Labrie Claude,
Breton Nathalie,
Rhéaume Eric,
Luu-The Van,
Labrie Fernand
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81516-9
Subject(s) - complementary dna , microbiology and biotechnology , biology , peptide sequence , nucleic acid sequence , cdna library , amino acid , protein primary structure , molecular cloning , homology (biology) , biochemistry , gene
We have used our recently characterized human 3β‐hydroxy‐5‐ene steroid dehydrogenase/Δ 5 ‐Δ 4 ‐isomerase (3β‐HSD) cDNA as probe to isolate cDNAs encoding bovine 3β‐HSD from a bovine ovary λgtll cDNA library. Nucleotide sequence analysis of two overlapping cDNA clones of 1362 bp and 1536 bp in length predicts a protein of 372 amino acids with a calculated molecular mass of 42093 (excluding the first Met). The deduced amino acid sequence of bovine 3β‐HSD displays 79% homology with human 3β‐HSD while the nucleotide sequence of the coding region shares 82% interspecies similarity. Hybridization of cloned cDNAs to bovine ovary poly(A) + RNA shows the presence of an approximately 1.7 kb mRNA species.