Bovine aortic actin shares similar physical properties with skeletal-muscle actin but differs in amino acid composition and ATPase activation.
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Aortic actin isoform differences are hypothesis-generating in animal models; leaves open relevance to human vascular myosin regulation.
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.
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Cavadore et al. (1985) studied this question.
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