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

The interaction of actin and myosin is considered to be a necessary condition for the contraction of striated muscle. A cytological demonstration that myosin can bind to a discrete part of the sarcomere, which from other evidence contains actin, was made by Huxley (1, p. 261). He observed an increase in phase contrast density when myosinextracted fibrils were treated wi th myosin in solution. Heavy meromyosin (HMM) , a protein fragment soluble at low ionic strength which is derived from the tryptic splitting of myosin, was also seen to bind. From electron microscope observations, Huxley (2) noted that this binding appears to be polarized. The present observations are an effort to increase the cytological sensitivity by which the binding of myosin is visualized and to give additional information on the localization of actin in striated muscle.

THE USE OF FLUORESCEIN-LABELED HEAVY MEROMYOSIN FOR THE CYTOLOGICAL DEMONSTRATION OF ACTIN