author_facet Cavadore, J C
Axelrud-Cavadore, C
Berta, P
Harricane, M C
Haiech, J
Cavadore, J C
Axelrud-Cavadore, C
Berta, P
Harricane, M C
Haiech, J
author Cavadore, J C
Axelrud-Cavadore, C
Berta, P
Harricane, M C
Haiech, J
spellingShingle Cavadore, J C
Axelrud-Cavadore, C
Berta, P
Harricane, M C
Haiech, J
Biochemical Journal
Preparation and characterization of bovine aortic actin
Cell Biology
Molecular Biology
Biochemistry
author_sort cavadore, j c
spelling Cavadore, J C Axelrud-Cavadore, C Berta, P Harricane, M C Haiech, J 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2280433 <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> Preparation and characterization of bovine aortic actin Biochemical Journal
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title Preparation and characterization of bovine aortic actin
title_unstemmed Preparation and characterization of bovine aortic actin
title_full Preparation and characterization of bovine aortic actin
title_fullStr Preparation and characterization of bovine aortic actin
title_full_unstemmed Preparation and characterization of bovine aortic actin
title_short Preparation and characterization of bovine aortic actin
title_sort preparation and characterization of bovine aortic actin
topic Cell Biology
Molecular Biology
Biochemistry
url http://dx.doi.org/10.1042/bj2280433
publishDate 1985
physical 433-441
description <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>
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author Cavadore, J C, Axelrud-Cavadore, C, Berta, P, Harricane, M C, Haiech, J
author_facet Cavadore, J C, Axelrud-Cavadore, C, Berta, P, Harricane, M C, Haiech, J, Cavadore, J C, Axelrud-Cavadore, C, Berta, P, Harricane, M C, Haiech, J
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description <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>
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imprint Portland Press Ltd., 1985
imprint_str_mv Portland Press Ltd., 1985
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spelling Cavadore, J C Axelrud-Cavadore, C Berta, P Harricane, M C Haiech, J 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2280433 <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> Preparation and characterization of bovine aortic actin Biochemical Journal
spellingShingle Cavadore, J C, Axelrud-Cavadore, C, Berta, P, Harricane, M C, Haiech, J, Biochemical Journal, Preparation and characterization of bovine aortic actin, Cell Biology, Molecular Biology, Biochemistry
title Preparation and characterization of bovine aortic actin
title_full Preparation and characterization of bovine aortic actin
title_fullStr Preparation and characterization of bovine aortic actin
title_full_unstemmed Preparation and characterization of bovine aortic actin
title_short Preparation and characterization of bovine aortic actin
title_sort preparation and characterization of bovine aortic actin
title_unstemmed Preparation and characterization of bovine aortic actin
topic Cell Biology, Molecular Biology, Biochemistry
url http://dx.doi.org/10.1042/bj2280433