Identification of myosin in a flowering plant, Egeria densa.
Copyright policy )Identification of myosin in a flowering plant, Egeria densa.
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 X 10(5). The presence of a heavy chain (MW = about 1.8 X 10(5)) 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.
Adenosine Triphosphatases, Molecular Weight, Kinetics, Muscles, Potassium, Myosins, Plants, Actins, Edetic Acid
Adenosine Triphosphatases, Molecular Weight, Kinetics, Muscles, Potassium, Myosins, Plants, Actins, Edetic Acid
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