Preparation and characterization of bovine aortic actin

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Bibliographische Detailangaben
Zeitschriftentitel:	Biochemical Journal
Personen und Körperschaften:	Cavadore, J C, Axelrud-Cavadore, C, Berta, P, Harricane, M C, Haiech, J
In:	Biochemical Journal, 228, 1985, 2, S. 433-441
Format:	E-Article
Sprache:	Englisch
veröffentlicht:	Portland Press Ltd.
Schlagwörter:	Cell Biology Molecular Biology Biochemistry

Details
Zusammenfassung:	<jats:p>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.</jats:p>
Umfang:	433-441
ISSN:	0264-6021 1470-8728
DOI:	10.1042/bj2280433