Partial amino acid sequence of a human seminal plasma peptide with inhibin‐like activity
Open Access
- 13 February 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 167 (1) , 98-102
Abstract
An extract of human seminal plasma was found to have inhibin‐like activity. The active factor was purified to homogeneity by ion exchange chromatography, molecular sieving and high performance liquid chromatography. The purified material has a mass of approximately 5 kDa and is very basic. Amino acid analysis showed the presence of approximately 35 residues while the sequencing data allowed the determination of the N‐terminal 31 amino acids. There is a possibility of an additional 2–4 residues at the C‐terminus, which could not be determined.Keywords
This publication has 15 references indexed in Scilit:
- Isolation and NH2-terminal sequence of a highly conserved human and porcine pituitary protein belonging to a new superfamilyArchives of Biochemistry and Biophysics, 1983
- Primary structure determination of Escherichia coli heat-stable enterotoxin of porcine originCanadian Journal of Biochemistry and Cell Biology, 1983
- Isolation and NH2‐terminal sequence of a novel porcine anterior pituitary polypeptideFEBS Letters, 1982
- ISOLATION AND CHARACTERIZATION OF INHIBIN FROM HUMAN SEMINAL PLASMA*Annals of the New York Academy of Sciences, 1982
- Progress in the isolation of inhibin like activity(ies) from different sources: A 1981 reportInternational Journal of Andrology, 1982
- MEASUREMENT OF NEURON‐SPECIFIC (NSE) AND NON‐NEURONAL (NNE) ISOENZYMES OF ENOLASE IN RAT, MONKEY AND HUMAN NERVOUS TISSUEJournal of Neurochemistry, 1979
- Inhibin — fact or artifactMolecular and Cellular Endocrinology, 1979
- Brain Enolases as Specific Markers of Neuronal and Glial CellsScience, 1978
- Evidence for inhibin-like activity in bovine follicular fluidNature, 1976
- Dual Endocrine Activity of the TestesScience, 1932