| Literature DB >> 134907 |
Abstract
Heavy meromyosin subfragment-1 (HMM S-1) was prepared by papain digestion of arterial myosin or actomyosin and was purified by agarose-ATP affinity chromatography. Proteolysis of crude arterial myosin suspensions was preceded by solubilization. HMM-S-1 thus obtained consisted mainly of a 90,000 dalton polypeptide and fully retained the K+- and Ca2+-ATPase of the parent myosin. Its affinity to agarose-ATP was comparable to that of skeletal muscle HMM S-1.Entities:
Mesh:
Substances:
Year: 1976 PMID: 134907 DOI: 10.1007/bf01927638
Source DB: PubMed Journal: Experientia ISSN: 0014-4754