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Characterization of a new bioactive protein from bovine seminal fluid.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1991 Sep 16; Vol. 179 (2), pp. 1006-10. - Publication Year :
- 1991
-
Abstract
- A new acidic seminal fluid protein (aSFP) was purified from bovine seminal fluid, using anion exchange chromatography and FPLC on MonoQ. The purified aSFP displays a pI of 4.8 and an apparent molecular weight of 14 kDa. Homogeneity of aSFP was demonstrated by FPLC and SDS-polyacrylamide gel electrophoresis. Monospecific anti-aSFP IgGs were employed to characterize aSFP in bovine seminal plasma and seminal vesicle secretion by immuno blot analysis. Proteinchemical characterization of aSFP included amino acid analysis as well as determination of 23 amino acid residues of the N-terminal sequence of aSFP. According to this sequence, aSFP appears to represent a hitherto unknown protein. aSFP stimulated cell division and progesterone secretion of bovine granulosa cells in vitro in a potent and dose dependent manner. aSFP appears to be a potent growth factor with effects on ovarian granulosa cells.
- Subjects :
- Amino Acid Sequence
Animals
Cattle
Cell Division
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Female
Male
Molecular Sequence Data
Molecular Weight
Progesterone metabolism
Proteins chemistry
Seminal Plasma Proteins
Prostatic Secretory Proteins
Proteins isolation & purification
Semen chemistry
Seminal Vesicles chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 179
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 1898381
- Full Text :
- https://doi.org/10.1016/0006-291x(91)91918-3