Literature DB >> 2760933

Antibody against the amino terminus of alpha-actin inhibits actomyosin interactions in the presence of ATP.

G DasGupta1, E Reisler.   

Abstract

Actomyosin interactions in the presence of ATP were examined by using site-specific antibodies directed against the first seven N-terminal residues on skeletal alpha-actin. Fab fragments of these antibodies (S alpha N Fab) inhibited effectively the actin-activated ATPase of myosin subfragment 1 (S-1) at both 5 and 25 degrees C. Binding experiments carried out in the presence of ATP at 5 degrees C revealed that the catalytic inhibition was related to the inhibition of S-1 binding to actin by Fab. At equimolar ratios of Fab to actin, the binding of S-1 to actin and the activated ATPase were inhibited by 75 and 82%, respectively. These results, when contrasted with the small effect of Fab on rigor actomyosin binding, suggest ATP-induced changes at the interface of actin and myosin.

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Year:  1989        PMID: 2760933     DOI: 10.1016/0022-2836(89)90249-0

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  21 in total

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Review 4.  Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation.

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7.  Localization of a myosin subfragment-1 interaction site on the C-terminal part of actin.

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8.  Small segmental rearrangements in the myosin head can explain force generation in muscle.

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9.  Characterization of an actin-myosin head interface in the 40-113 region of actin using specific antibodies as probes.

Authors:  J P Labbé; C Méjean; Y Benyamin; C Roustan
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10.  Cross-bridge binding to actin and force generation in skinned fibers of the rabbit psoas muscle in the presence of antibody fragments against the N-terminus of actin.

Authors:  B Brenner; T Kraft; G DasGupta; E Reisler
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