Leucocyte myosin and its location in the cell.
The intracellular location of the binding site of antibody against purified myosin prepared from equine leucocytes was investigated in neutrophils and lymphocytes by electron microscopy using peroxidase-labelled antibody method. The myosin extracted from equine leucocytes could bind skeletal muscle F-actin and the formed complex showed the biophysical and biochemical properties and electron microscopic appearance of actomyosin. On immunodiffusion, the leucocyte myosin formed a single precipitin line with its antibody prepared in rabbits. The antibody also formed single precipitin lines with myosins from lymphocytes and thrombocytes, fusing with each other. The antibody against the leucocyte myosin did not react with myosins from skeletal or arterial smooth muscle. The specificity of the antibody was further established by determination of K+-EDTA-activated ATPase activity remained in the supernate of antigen-antibody mixture. Under electron microscope, the intracellular immunoreactive products of peroxidase labelled antibody were found in cytoplasm of neutrophils and lymphocytes incubated with antibody against leucocyte myosin, but not in neutrophils or lymphocytes treated with IgG from normal rabbits.
D000251:Adenosine Triphosphatases / Q000097:blood; D000818:Animals; D006736:Horses; D007962:Leukocytes / Q000032:analysis* / Q000201:enzymology / Q000648:ultrastructure; D008858:Microscopy, Phase-Contrast; D009218:Myosins / Q000097:blood* / Q000276:immunology; D009504:Neutrophils / Q000032:analysis / Q000648:ultrastructure; D013347:Subcellular Fractions / Q000032:analysis
D000251:Adenosine Triphosphatases; D009218:Myosins