Preparation and characterization of bovine aortic actin.
A functional vascular smooth-muscle actin from bovine aorta was purified to homogeneity by an original method and was able to polymerize. Aortic actin is composed of two major isoforms and at least two minor ones. This actin was not phosphorylated by either cyclic AMP-dependent protein kinase or C kinase. The physical properties of aortic actin were found to be very similar to those of skeletal-muscle actin, except for amino acid composition (three tryptophan residues instead of four). The aortic actin and skeletal-muscle actin differ in the extent of activation of the Mg-dependent ATPase of skeletal-muscle myosin.
Cavadore
J C
JC
Axelrud-Cavadore
C
C
Berta
P
P
Harricane
M C
MC
Haiech
J
J
D000199:Actins / Q000302:isolation & purification / Q000494:pharmacology; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001011:Aorta / Q000032:analysis; D017301:Ca(2+) Mg(2+)-ATPase; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D004789:Enzyme Activation / Q000187:drug effects; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D009131:Muscle, Smooth, Vascular / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D010766:Phosphorylation
D000199:Actins; D000596:Amino Acids; D046911:Macromolecular Substances; D010446:Peptide Fragments; D010450:Endopeptidases; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase