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.
| Original language | English |
|---|---|
| Pages (from-to) | 1221-1222 |
| Number of pages | 2 |
| Journal | Experientia |
| Volume | 32 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 1976 |
| Externally published | Yes |