Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms
Author:
Affiliation:
1. Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, VT 05405, USA
Publisher
Wiley
Subject
Physiology
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1469-7793.1999.0669n.x
Reference46 articles.
1. Reduced cardiac myofibrillar Mg-ATPase activity without changes in myosin isozymes in patients with end-stage heart failure
2. Increased myothermal economy of isometric force generation in compensated cardiac hypertrophy induced by pulmonary artery constriction in the rabbit. A characterization of heat liberation in normal and hypertrophied right ventricular papillary muscles.
3. Shortening velocity and myosin and myofibrillar ATPase activity related to myosin isoenzyme composition during postnatal development in rat myocardium.
4. Reversal of the cross-bridge force-generating transition by photogeneration of phosphate in rabbit psoas muscle fibres.
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