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PMID: 3160341 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Preparation and characterization of bovine aortic actin.

The Biochemical journal ·Vol. 228 ·No. 2 ·1985-06-01 ·Pages 433-41

Cavadore JC, Axelrud-Cavadore C, Berta P, Harricane MC, Haiech J

Abstract

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.

MeSH Terms
Actins/isolation & purification,pharmacology Adenosine Triphosphatases/metabolism Amino Acids/analysis Animals Aorta/analysis Ca(2+) Mg(2+)-ATPase Cattle Electrophoresis, Polyacrylamide Gel Endopeptidases Enzyme Activation/drug effects Macromolecular Substances Microscopy, Electron Muscle, Smooth, Vascular/analysis Peptide Fragments/analysis Phosphorylation
Chemicals
Actins Amino Acids Macromolecular Substances Peptide Fragments Endopeptidases Adenosine Triphosphatases Ca(2+) Mg(2+)-ATPase
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Cavadore J C
Axelrud-Cavadore C
Berta P
Harricane M C
Haiech J
References (34)
34 references, click to expand
  1. A model for the myosin molecule.
    Biochim Biophys Acta. 1960 Jul 15;41:401-21 PMID: 14408979
  2. Methods to measure actin polymerization.
    Methods Enzymol. 1982;85 Pt B:182-210 PMID: 6889668
  3. The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence.
    J Biol Chem. 1975 Aug 10;250(15):5915-20 PMID: 1150665
  4. Cleavage of structural proteins during the assembly of the head of bacteriophage T4.
    Nature. 1970 Aug 15;227(5259):680-5 PMID: 5432063
  5. Activation of smooth muscle myosin by smooth and skeletal muscle actins.
    FEBS Lett. 1981 Nov 16;134(2):197-202 PMID: 6118302
  6. A protein sequenator.
    Eur J Biochem. 1967 Mar;1(1):80-91 PMID: 6059350
  7. Phosphorylation of smooth muscle actin by the catalytic subunit of the cAMP-dependent protein kinase.
    Biochem Biophys Res Commun. 1981 Sep 16;102(1):149-57 PMID: 6272789
  8. Selective precipitation of 32Pi onto filter papers. Application to ATPase and cyclic AMP phosphodiesterase determination.
    Biochim Biophys Acta. 1978 Apr 12;523(2):516-21 PMID: 207336
  9. Effect of phosphorylation on the actin-activated ATPase activity of myosin.
    Biochem Biophys Res Commun. 1981 Feb 12;98(3):800-5 PMID: 6452877
  10. Amino acid sequence of Acanthamoeba actin.
    J Mol Biol. 1984 Jan 5;172(1):141-7 PMID: 6420574
  11. The amino acid sequence of actin from chicken skeletal muscle actin and chicken gizzard smooth muscle actin.
    FEBS Lett. 1979 Jun 15;102(2):219-22 PMID: 456601
  12. Chicken-gizzard actin: polymerization and stability.
    Eur J Biochem. 1980 Feb;104(1):41-52 PMID: 6445264
  13. A NEW PROTEIN COMPONENT PARTICIPATING IN THE SUPERPRECIPITATION OF MYOSIN B.
    J Biochem. 1964 Jun;55:604-13 PMID: 14216404
  14. THIRD COMPONENT PARTICIPATING IN THE SUPERPRECIPITATION OF 'NATURAL ACTOMYOSIN'.
    Nature. 1963 Dec 7;200:1010 PMID: 14097720
  15. G-actin modified by plasma membrane interaction polymerizes only in the presence of filamentous myosin.
    FEBS Lett. 1980 Mar 24;112(1):67-9 PMID: 6892805
  16. Relationships of the spectrin complex of human erythrocyte membranes to the actomyosins of muscle cells.
    Biochemistry. 1976 Oct 5;15(20):4486-92 PMID: 135578
  17. Biochemical and structural characterization of actin from Dictyostelium discoideum.
    J Biol Chem. 1978 Dec 25;253(24):9088-96 PMID: 152763
  18. Regulation of the actin-myosin interaction in vertebrate smooth muscle: activation via a myosin light-chain kinase and the effect of tropomyosin.
    J Mol Biol. 1977 Jun 5;112(4):559-76 PMID: 195061
  19. Preparation and properties of vertebrate smooth-muscle myofibrils and actomyosin.
    Eur J Biochem. 1975 Jun 16;55(1):49-60 PMID: 126155
  20. Amino acid analysis and peptide mapping of bovine carotid actin.
    Biochim Biophys Acta. 1969 Feb 4;175(1):165-73 PMID: 5766000
  21. Silver staining of proteins in polyacrylamide gels.
    Anal Biochem. 1981 Nov 15;118(1):197-203 PMID: 6175245
  22. Purification of muscle actin.
    Methods Enzymol. 1982;85 Pt B:164-81 PMID: 7121269
  23. The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation.
    Differentiation. 1979;14(3):123-33 PMID: 499690
  24. Refinement of the coomassie blue method of protein quantitation. A simple and linear spectrophotometric assay for less than or equal to 0.5 to 50 microgram of protein.
    Anal Biochem. 1978 May;86(1):142-6 PMID: 655375
  25. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.
    J Biol Chem. 1971 Aug 10;246(15):4866-71 PMID: 4254541
  26. A rapid microdetermination of phosphoserine, phosphothreonine, and phosphotyrosine in proteins by automatic cation exchange on a conventional amino acid analyzer.
    Anal Biochem. 1983 Jan;128(1):206-12 PMID: 6189415
  27. Actin from pig and rat uterus.
    Biochem J. 1981 Mar 1;193(3):891-8 PMID: 6458278
  28. High resolution two-dimensional electrophoresis of proteins.
    J Biol Chem. 1975 May 25;250(10):4007-21 PMID: 236308
  29. Phosphorylation of rabbit muscle troponin and actin by a 3', 5'-c-AMP-dependent protein kinase.
    FEBS Lett. 1972 Oct 15;27(1):89-93 PMID: 11946814
  30. Automated method for the quantitation of orthophosphate.
    Anal Biochem. 1976 Oct;75(2):447-53 PMID: 984405
  31. Complete amino acid analysis of proteins from a single hydrolysate.
    J Biol Chem. 1976 Apr 10;251(7):1936-40 PMID: 178649
  32. Adenosine 3':5'-monophosphate dependent protein kinase from bovine heart. Characterization of the catalytic subunit.
    Biochemistry. 1977 Dec 27;16(26):5691-7 PMID: 201274
  33. Phosphorylation of actin and removal of its inhibitory activity on pancreatic DNAase I by liver plasma membranes.
    FEBS Lett. 1979 Aug 15;104(2):284-6 PMID: 477988
  34. Separation of subfragment-1 isoenzymes from rabbit skeletal muscle myosin.
    Nature. 1975 Sep 4;257(5521):54-6 PMID: 125854
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2280433
Published
1985-06-01
Pages
433-41
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1145001
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2280433 PMC Full Text View journal details
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