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

Dancker, Peter

doi:10.1016/0167-4838(83)90239-X

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

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

MPS-Authors

/persons/resource/persons205722

Dancker, Peter
Max Planck Institute for Medical Research, Max Planck Society;

External Resource

https://www.sciencedirect.com/science/article/pii/016748388390239X/pdf?md5=29cbf23a11a4c324ad20c721328c590c&pid=1-s2.0-016748388390239X-main.pdf
(Any fulltext)

https://doi.org/10.1016/0167-4838(83)90239-X
(Any fulltext)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

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.

Cite as: https://hdl.handle.net/21.11116/0000-0003-637D-2

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.