IDENTIFICATION OF MYOSIN IN A FLOWERING PLANT, EGERIA-DENSA

A myosin-like protein was extracted and partially purified from a flowering plant, E. densa. It had no p-nitrophenyl phosphatase activity, but exhibited EDTA(K+)-ATPase [EC 3.6.1.3] activity at high ionic strength. Its MW as estimated by gel filtration was 4-5 .times. 105. The presence of a heavy chain (MW = about 1.8 .times. 105) was indicated by SDS-gel electrophoresis. Egeria myosin aggregated in an environment of low ionic strength and formed bipolar filaments. It bound with skeletal muscle F-actin with a periodicity of 40 nm.