title: Purification and kinetic properties of protein kinase C from cultured smooth muscle cells.
abstract: Protein kinase C has been purified from in vitro cultures of A7r5 vascular smooth muscle cells. Three substrates have been employed for the kinetic analysis of the enzyme, Histone III-S, FKKSFKL-NH2 (analogous of the pseudo-substrate of the enzyme) and MBP4-14 (part of basic myelin protein) protein. The enzyme activity depends not only on the PKC-specific sequence motif, common to the three substrates, but also on additional structural motifs, which may be important also in governing the substrate selectivity of the enzyme in vivo.
authors.affiliation: Institut für Biochemie und Molekularbiologie, Universität Bern, Switzerland.
authors.forename: B
authors.initials: B
authors.lastname: Stäuble
authors.forename: D
authors.initials: D
authors.lastname: Boscoboinik
authors.forename: A
authors.initials: A
authors.lastname: Azzi
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001011:Aorta; D002478:Cells, Cultured; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism; D015151:Immunoblotting; D007700:Kinetics; D008969:Molecular Sequence Data; D009131:Muscle, Smooth, Vascular / Q000166:cytology / Q000201:enzymology*; D004676:Myelin Basic Protein / Q000378:metabolism; D011493:Protein Kinase C / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D051381:Rats; D013379:Substrate Specificity
chemical_list: D006657:Histones; D004676:Myelin Basic Protein; D011493:Protein Kinase C