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Complete amino acid sequence of human placental 17β‐hydroxysteroid dehydrogenase deduced from cDNA
Author(s) -
Peltoketo H.,
Isomaa V.,
Mäentausta O.,
Vihko R.
Publication year - 1988
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(88)80548-9
Subject(s) - complementary dna , nucleic acid sequence , peptide sequence , microbiology and biotechnology , open reading frame , amino acid , biology , biochemistry , cdna library , coding region , polyclonal antibodies , nucleotide , protein primary structure , gene , genetics , antibody
CDNA clones for 17β‐hydroxysteroid dehydrogenase (17‐HSD; EC 1.1.1.62) were isolated from a placental λgt11 expression library using polyclonal antibodies against placental 17‐HSD. The largest cDNA contained 1325 nucleotides, consisting of a short 5′‐noncoding segment, a coding segment of 987 nucleotides terminated by a TAA codon, and a 329 nucleotide long 3′‐noncoding segment. The open reading frame encoded a polypeptide of 327 amino acid residues with a predicted M r of 34853. The amino acid sequence of 23 N‐terminal amino acids determined from purified 17‐HSD agreed with the sequence deduced from cDNA. The deduced amino acid sequence also contained two peptides previously characterized from the proposed catalytic area of placental 17‐HSD.