ArticlePflugers Archiv : European journal of physiology1992
Active movement of cardiac myosin on Characeae actin cables.
Article in Pflugers Archiv : European journal of physiology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 9 citations in OpenAlex.
- Mitochondrial colocalization with Ca2+ release sites is crucial to cardiac metabolism.Biophysical journal · 2013Article
- Link between the enzymatic kinetics and mechanical behavior in an actomyosin motor.Biophysical journal · 2001Article
- Depressed sliding velocity of isolated cardiac myosin from cardiomyopathic hamsters: evidence for an alteration in mechanical interaction of actomyosin.Molecular and cellular biochemistry · 1993Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The active sliding of cardiac myosin on actin cables was studied using an in vitro movement assay. Cardiac myosin prepared from either adult rabbit or rat hearts was mixed with small latex beads to coat them. Actin cables were obtained from the internodal cells of green algae, Characeae. When the myosin-coated beads suspended in physiological buffer were introduced into the internodal cells, the myosin started to interact with the actin causing the beads to move. The sliding movement of the beads was observed under microscopy and the sliding velocity measured. The observed movement was smooth and the velocity was constant over a long distance. The movement was physiological in nature: a) it was ATP-dependent, but above a certain level of ATP, the velocity was constant; b) the velocity was maximum at pH 7.0, and decreased in both acidic and alkaline conditions. The average sliding velocity of cardiac myosin obtained from rabbit ventricles (0.31 +/- 0.11 micron/s) was slower than that from rat ventricles (1.04 +/- 0.26 micron/s) reflecting the lower ATPase activity of rabbit cardiac myosin. This assay system is considered to be a useful tool linking biochemistry and physiology at the molecular level.
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Registered trials
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