Literature DB >> 7278859

Effect of Cibachron Blue F3GA on the polymerization of actin.

V P Shanbhag, L Backman, G Pinaev.   

Abstract

The effect of the dye Cibachron Blue F3GA on the G-F transformation of rabbit muscle actin has been studied with viscosimetry. The presence of the dye which is known to bind to nucleotide binding sites, decreased both the initial rate of polymerization of actin as well as the final viscosity of actin. Both these effects can be ascribed to an increase in the critical concentration of actin. The inhibitory effect of Cibachron Blue F3GA was counteracted by ATP, suggesting a competition between Cibachron Blue F3GA and ATP for the binding site/sites on actin.

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Year:  1981        PMID: 7278859     DOI: 10.1007/BF02354930

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  11 in total

1.  Depolymerisation of F-actin to G-actin and its repolymerisation in the presence of analogs of adenosine triphosphate.

Authors:  H G Mannherz; H Brehme; U Lamp
Journal:  Eur J Biochem       Date:  1975-12-01

2.  POLYMERIZATION OF ACTIN FREE FROM NUCLEOTIDES AND DIVALENT CATIONS.

Authors:  M KASAI; E NAKANO; F OOSAWA
Journal:  Biochim Biophys Acta       Date:  1965-03-29

3.  Interactions of contractile proteins with free and immobilized cibacron Blue F3GA.

Authors:  A P Toste; R Cooke
Journal:  Anal Biochem       Date:  1979-06       Impact factor: 3.365

4.  Head to tail polymerization of actin.

Authors:  A Wegner
Journal:  J Mol Biol       Date:  1976-11       Impact factor: 5.469

5.  Interaction of actin with analogs of adenosine triphosphate.

Authors:  R Cooke; L Murdoch
Journal:  Biochemistry       Date:  1973-09-25       Impact factor: 3.162

6.  Troponin-tropomyosin complex. Column chromatographic separation and activity of the three, active troponin components with and without tropomyosin present.

Authors:  E Eisenberg; W W Kielley
Journal:  J Biol Chem       Date:  1974-08-10       Impact factor: 5.157

7.  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.

Authors:  J A Spudich; S Watt
Journal:  J Biol Chem       Date:  1971-08-10       Impact factor: 5.157

8.  Complete amino-acid sequence of actin of rabbit skeletal muscle.

Authors:  M Elzinga; J H Collins; W M Kuehl; R S Adelstein
Journal:  Proc Natl Acad Sci U S A       Date:  1973-09       Impact factor: 11.205

9.  Substoichiometric concentrations of cytochalasin D inhibit actin polymerization. Additional evidence for an F-actin treadmill.

Authors:  S L Brenner; E D Korn
Journal:  J Biol Chem       Date:  1979-10-25       Impact factor: 5.157

Review 10.  The polymerization reaction of muscle actin.

Authors:  J Engel; H Fasold; F W Hulla; F Waechter; A Wegner
Journal:  Mol Cell Biochem       Date:  1977-11-25       Impact factor: 3.396

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