Isotypes of protein kinase C in bovine sperm.
Protein kinase C is present in bovine epididymal sperm. The enzyme was partially purified by gel filtration on Sephacryl S-300. The Ca2+/phosphatidylserine-dependent histone phosphotransferase activity elutes from the gel filtration column in a manner corresponding to a Mr approximately 80 kDa. The activity peak also corresponds with [3H]phorbol 12,13-dibutyrate binding activity. Immunoblot analysis of the partially purified enzyme with isozyme-specific monoclonal antibodies revealed the presence of alpha-, beta-, and gamma-subspecies of protein kinase C. Indirect immunofluorescence showed that the antibodies against alpha-, beta-, and gamma-subspecies produced prominent staining of the postacrosomal region of the sperm head. In addition, beta-subspecies antibodies produced minor staining of the midpiece and gamma-subspecies antibodies produced a minor staining of the acrosomal region.
Chaudhry
P S
PS
Department of Chemistry, New Mexico State University, Las Cruces 88003.
Casillas
E R
ER
D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002850:Chromatography, Gel; D005455:Fluorescent Antibody Technique; D007527:Isoenzymes / Q000378:metabolism*; D008297:Male; D015240:Phorbol 12,13-Dibutyrate / Q000378:metabolism; D011493:Protein Kinase C / Q000378:metabolism*; D013094:Spermatozoa / Q000201:enzymology*
D007527:Isoenzymes; D015240:Phorbol 12,13-Dibutyrate; D011493:Protein Kinase C