Abstract
Cardiac myosin was obtained from the hearts of normal dogs by conventional extraction and precipitation techniques, followed by ammonium sulfate fractionation in the presence of 2.0 M lithium chloride. The molecular characteristics of this protein preparation are presented. Cardiac myosin prepared by this technique shows less tendency than conventionally prepared solutions to denature when stored at 0 to 4°C, and has a significantly higher ATP ase activity. Comparison of canine cardiac myosin and skeletal muscle myosin, obtained under identical conditions, revealed no differences between these two proteins in their intrinsic viscosities, S 20. w , molecular weight, and UV absorbances, although ATP ase activity was lower for cardiac myosin.
Sign-in/Register to access full text options 
Free) 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
