English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Tools annual

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Presents the access of premium content as premium feature

Premium Content

Global: Zendy Plus annual

Global: Zendy Free Plan

The binding of the Ca2+-regulated native thin filaments from vascular smooth muscle to vascular smooth-muscle heavy meromyosin was measured in the presence of 3 mM-MgATP. At 25 degrees C and I 0.25 binding had an affinity of 1 X 10(-6)-0.3 X 10(-6) M-1 with a stoichiometry of one molecule bound to one actin monomer. The Km for the activation of heavy-meromyosin ATPase was 20-50 microM. Thin filament-heavy meromyosin binding was not altered by Ca2+ (pCa 9-4) or the extent of myosin phosphorylation. With skeletal-muscle heavy meromyosin affinity was 0.023 X 10(6) M-1 in parallel with activation of the ATPase (Km 54 microM). It is concluded that tight binding is specific to smooth-muscle proteins and that it is not related to the ATPase activation site.

A tight-binding interaction between smooth-muscle native thin filaments and heavy meromyosin in the presence of MgATP