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 Plus annual

Presents the access of premium content as premium feature

Premium Content

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 annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

1. Electrophoretically homogeneous calcium-sensitizing factor was prepared from the troponin complex by chromatography successively on sulphoethyl-Sephadex and on diethyl-(2-hydroxypropyl)aminoethyl-Sephadex in 6m-urea. It is a protein containing 53% of polar amino acids, of which a net excess consists of acidic residues. 2. On gel filtration the calcium-sensitizing factor was shown to be the only myofibrillar protein that bound (45)Ca(2+) tightly in the presence of 2-6m-urea. 3. Calcium-sensitizing factor effectively neutralized the effect of the inhibitory factor on the ATPase activities of actomyosin systems. Tropomyosin was essential for the regulation, by changes in the Ca(2+) concentration, of the neutralizing effect of calcium-sensitizing factor on the inhibitory factor. 4. Prolonged exposure to chelators of Ca(2+) produced an irreversibly modified form of calcium-sensitizing factor of higher electrophoretic mobility at pH8.6. The modified form neutralized the inhibitory factor action but this property could no longer be controlled by the Ca(2+) concentration in the presence of tropomysin. 5. The calcium-sensitizing factor and tropomyosin could be replaced by their carboxymethylated derivatives in the relaxing-protein system.

The regulatory proteins of the myofibril. Characterization and biological activity of the calcium-sensitizing factor (troponin A)