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The Regulation of Rabbit Skeletal Muscle Contraction

Journal of Biological Chemistry · 1971 · Vol. 246(15) · pp. 4866–4871
James A. SpudichSusan Watt

Abstract

Actin purified by a new, simple, and rapid purification procedure activated the ATPase activity of both heavy meromyosin and Subfragment 1 of heavy meromyosin, and this activation was not inhibited by the removal of Ca2+. Preparations of tropomyosin-troponin inhibited (by 85%) both the acto-heavy meromyosin and acto-Subfragment 1 ATPases in the absence of, but not in the presence of, Ca2+. This inhibition was shown to result from binding of the tropomyosin-troponin complex solely to actin and in a ratio of about 1 mole of tropomyosin-troponin to 7 moles of actin.

Cardiomyopathy and Myosin StudiesMuscle Physiology and DisordersCardiovascular Effects of ExerciseSkeletal muscleRabbit (cipher)Contraction (grammar)Muscle contractionCell biologyChemistryAnatomyBiologyEndocrinologyComputer science

MeSH terms

ActinsAdenosine TriphosphatasesAdenosine TriphosphateQuaternary Ammonium CompoundsAnimalsCalcium ChlorideChromatography, GelElectrophoresisEnzyme ActivationKineticsMathematicsMercaptoethanolMuscle ContractionMuscle ProteinsMyosins
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References
PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT
Journal of Biological Chemistry · 1951 · 317,666 citations
THE COLORIMETRIC DETERMINATION OF PHOSPHORUS
Journal of Biological Chemistry · 1925 · 19,069 citations
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