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  The competition between adenosine triphosphate and inorganic pyrophosphate for myosin and its suppression by substoichiometric actin concentrations

Dancker, P. (1983). The competition between adenosine triphosphate and inorganic pyrophosphate for myosin and its suppression by substoichiometric actin concentrations. Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology, 749(3), 296-301. doi:10.1016/0167-4838(83)90239-X.

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BBA_749_1983_296.pdf (Any fulltext), 392KB
 
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 Creators:
Dancker, Peter1, Author           
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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Free keywords: Myosin subfragment 1; Pyrophosphate; ATPase; Actin-myosin interaction; Fluorescence change; (Rabbit sketal muscle)
 Abstract: Inorganic pyrophosphate (PPi) inhibits not only Mg2+-ATPase activity of myosin subfragment 1 (S-1) but abolishes also the ATP-induced increment of tryptophan fluorescence of subfragment 1. At the concentrations used (25-50 micron ATP, 12 mm PPi) these effects of PPi were abolished by substoichiometric actin concentrations (approx. 0.1 microM actin vs. approx. 1 microM S-1), where ATPase activity was barely stimulated by actin.

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Language(s): eng - English
 Dates: 1983-06-172003-01-221983-12-28
 Publication Status: Issued
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
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Title: Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 749 (3) Sequence Number: - Start / End Page: 296 - 301 Identifier: ISSN: 0167-4838
CoNE: https://pure.mpg.de/cone/journals/resource/954925482647