Characterization of a cDNA coding for sex steroid-binding protein of human plasma
Abstract
A cDNA (912 nucleotides) coding for human plasma sex steroid-binding protein (SBP) was characterized from a phage clone previously isolated by screening a Charon 21A human liver cDNA library with rat androgen binding protein (ABP) cDNA. The deduced amino acid sequence from the cDNA indicated that the insert was a partial clone coding for 281 amino acids starting with residue 92 (glycine) encompassing the alternating leucyl residues and the carboxyl-end 373 (histidine) as previously reported [(1986) Biochemistry 25, 7584]. The potential polyadenylation signal sequence ATTAAA is present as part of the 3‧-coding region and the stop codon TAA. Both are followed by a short 20 untranslated nucleotides and a poly(A) tract of 49 nucleotides. Significant homologous sequences (76%) at the DNA level exist between human SBP and rat ABP which might suggest the possibility that both evolved from a common primordial gene. Demonstration of the presence of an SBP cDNA in a human liver cDNA library provides the first evidence that liver is the site of SBP biosynthesis.
- Publication:
-
FEBS Letters
- Pub Date:
- January 1987
- DOI:
- 10.1016/0014-5793(87)80261-2
- Bibcode:
- 1987FEBSL.219..405Q
- Keywords:
-
- Steroid-binding protein;
- cDNA;
- Amino acid sequence;
- (Human plasma)