Cloning and sequence analysis of cDNA species coding for the two subunits of inhibin from bovine follicular fluid.
- 1 May 1986
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 83 (10) , 3091-3095
- https://doi.org/10.1073/pnas.83.10.3091
Abstract
The primary amino acid structures of the 43-kDa (A) and 15-kDa (B) subunits of the 58-kDa form of the hormone inhibin have been elucidated by cloning and analysis of cDNA species derived from bovine granulosa cell mRNA. The A subunit (Mr = 32,298) is a protein of 300 amino acids with two potential N-glycosylation sites and two potential proteolytic processing sites and has a pre-pro region of 60 amino acids. The mature B subunit (Mr = 12,977) is a protein of 116 amino acids synthesized from a separate mRNA. These data establish that a 31-kDa form of inhibin also isolated from bovine follicular fluid, with subunits of 20 kDa (Ac) and 15 kDa (B), is derived from the 58-kDa form by proteolytic processing of the A subunit.This publication has 27 references indexed in Scilit:
- Studies on transformation of Escherichia coli with plasmidsPublished by Elsevier ,2006
- Isolation of porcine follicular fluid inhibin of 32K daltonsBiochemical and Biophysical Research Communications, 1985
- Amino acid sequence of the predominant basic protein in human seminal plasmaFEBS Letters, 1985
- Isolation and characterization of genomic and cDNA clones of human erythropoietinNature, 1985
- Isolation of inhibin from bovine follicular fluidBiochemical and Biophysical Research Communications, 1985
- Analysis of an inhibin preparation reveals apparent identity between a peptide with inhibin‐like activity and a sperm‐coating antigenFEBS Letters, 1984
- Complete amino acid sequence of human seminal plasma β‐inhibinFEBS Letters, 1984
- Sugar Residues on ProteinCritical Reviews in Biochemistry, 1981
- PROCESSING MECHANISMS IN THE BIOSYNTHESIS OF PROTEINS*Annals of the New York Academy of Sciences, 1980
- Isolation of biologically active ribonucleic acid from sources enriched in ribonucleaseBiochemistry, 1979