Identification of Myosin in a Flowering Plant, Egeria densa

Abstract

A myosin-like protein was extracted and partially purified from a flowering plant, Egeria densa. It had no p-nitrophenyl phosphatase activity, but exhibited EDTA(K⁺)-ATPase [EC 3. 6. 1. 3] activity at high ionic strength. Its molecular weight as estimated by gel filtration was 4-5×10⁵. The presence of a heavy chain (MW=about 1.8×10⁵) 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 40nm.