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Molecular cloning and sequence of the cDNA for a 94-amino-acid seminal plasma protein secreted by the human prostate.

Authors
  • Mbikay, M
  • Nolet, S
  • Fournier, S
  • Benjannet, S
  • Chapdelaine, P
  • Paradis, G
  • Dubé, J Y
  • Tremblay, R
  • Lazure, C
  • Seidah, N G
Type
Published Article
Journal
DNA (Mary Ann Liebert, Inc.)
Publication Date
Feb 01, 1987
Volume
6
Issue
1
Pages
23–29
Identifiers
PMID: 3829888
Source
Medline
License
Unknown

Abstract

The precursor to a seminal plasma protein reported to have inhibin-like activity was characterized through cDNA cloning and sequencing. It is a 114-amino-acid polypeptide which differs from its seminal plasma derivative mainly by the presence of a 20-residue amino-terminal extension, a putative signal sequence, carrying a possible N-glycosylation site. The protein is specified by a single gene per haploid genome. Its mRNA is detectable in the prostate but not in the testis, which suggests that it is primarily a prostatic secretory protein.

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