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.
D000199:Actins; D000251:Adenosine Triphosphatases / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D007700:Kinetics; D008970:Molecular Weight; D009132:Muscles; D009218:Myosins / Q000032:analysis*; D010944:Plants / Q000201:enzymology*; D011188:Potassium / Q000494:pharmacology
D000199:Actins; D004492:Edetic Acid; D000251:Adenosine Triphosphatases; D009218:Myosins; D011188:Potassium