Characterization of rat parotid protein kinase C.
1. Protein kinase C (PK-C) from the rat parotid gland has been partially purified and characterized for the first time. During its purification, this enzyme exhibited the same chromatographic behavior as the rat brain enzyme. 2. Affinities for phosphatidylserine (3 micrograms/ml), ATP (8 microM) and calcium (8 microM) were determined kinetically and found to be similar for the enzymes from each tissue. 3. Experiments designed to detect agonist-stimulated translocation of PK-C activity during phosphatidylinositol turnover found no change in levels of soluble PK-C, suggesting that PK-C translocation may not be an obligatory correlate of its activation. The implications of this result are discussed.
Hincke
M T
MT
Department of Anatomy, University of Ottawa, Ontario, Canada.
D000818:Animals; D002217:Carbachol / Q000494:pharmacology; D003600:Cytosol / Q000201:enzymology; D066298:In Vitro Techniques; D007545:Isoproterenol / Q000494:pharmacology; D008297:Male; D010306:Parotid Gland / Q000187:drug effects / Q000201:enzymology* / Q000378:metabolism; D010656:Phenylephrine / Q000494:pharmacology; D011493:Protein Kinase C / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D010656:Phenylephrine; D002217:Carbachol; D011493:Protein Kinase C; D007545:Isoproterenol