Literature DB >> 3734052

A kinetic comparison between Mg-actin and Ca-actin.

L A Selden, L C Gershman, J E Estes.   

Abstract

The kinetics of the elongation reaction in the polymerization of actin containing tightly-bound Mg2+ (Mg-actin) or tightly-bound Ca2+ (Ca-actin) have been studied. The reaction was monitored using the increase in fluorescence intensity of N-(1-pyrenyl)iodoacetamide-labelled monomeric actin as a measure of polymer formation. The actin nucleation reaction was circumvented by the addition of phalloidin-stabilized actin nuclei. Elongation rates were obtained at various actin concentrations and at various temperatures for polymerization induced by the presence of different monovalent and divalent salt concentrations. Values for the relative rate constant of forward polymerization (mk+) for Mg-actin were found to be larger than those for Ca-actin under similar conditions (m = number of polymer ends). The critical actin concentration (Cc) of Mg-actin is lower than the Cc for Ca-actin, as were estimates of the relative rate constant of depolymerization (mk-). The temperature dependence of Cc, mk+ and mk- for Mg-actin was different from that for Ca-actin, further suggesting a difference in monomeric properties due to the type of divalent cation tightly bound to actin. Estimates of the activation enthalpy change for the forward reaction in the G in equilibrium F transformation were similar for both types of actin, but the activation enthalpy change for the depolymerization of Mg-actin was significantly larger than that for Ca-actin.

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Year:  1986        PMID: 3734052     DOI: 10.1007/bf01753554

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  24 in total

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Authors:  L A Selden; J E Estes; L C Gershman
Journal:  Biochem Biophys Res Commun       Date:  1983-10-31       Impact factor: 3.575

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Authors:  L S Tobacman; E D Korn
Journal:  J Biol Chem       Date:  1983-03-10       Impact factor: 5.157

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  9 in total

Review 1.  Tightly-bound divalent cation of actin.

Authors:  J E Estes; L A Selden; H J Kinosian; L C Gershman
Journal:  J Muscle Res Cell Motil       Date:  1992-06       Impact factor: 2.698

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Authors:  W P Shu; D Wang; A Stracher
Journal:  Biochem J       Date:  1992-04-15       Impact factor: 3.857

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Authors:  F Wang; R V Sampogna; B R Ware
Journal:  Biophys J       Date:  1989-02       Impact factor: 4.033

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Authors:  H Strzelecka-Golaszewska; A Wozniak; T Hult; U Lindberg
Journal:  Biochem J       Date:  1996-06-15       Impact factor: 3.857

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Authors:  M O Steinmetz; K N Goldie; U Aebi
Journal:  J Cell Biol       Date:  1997-08-11       Impact factor: 10.539

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Authors:  M Mossakowska; J Moraczewska; S Khaitlina; H Strzelecka-Golaszewska
Journal:  Biochem J       Date:  1993-02-01       Impact factor: 3.857

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Authors:  I DalleDonne; A Milzani; R Colombo
Journal:  Biophys J       Date:  1995-12       Impact factor: 4.033

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Authors:  A Laliberte; C Gicquaud
Journal:  J Cell Biol       Date:  1988-04       Impact factor: 10.539

9.  The Dictyostelium discoideum 30,000-dalton protein is an actin filament-bundling protein that is selectively present in filopodia.

Authors:  M Fechheimer
Journal:  J Cell Biol       Date:  1987-06       Impact factor: 10.539

  9 in total

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