Electron microscopy of scallop myosin. Location of regulatory light chains.
The heads of the Ca2+-sensitive myosin molecules from scallop muscle, contrasted for electron microscopy by rotary shadowing, display two appearances depending on the presence or absence of the regulatory light chains. The heads of intact myosin appear "pear-shaped" as described for vertebrate myosin (Elliott & Offer, 1978): they are widest at the end remote from the tail and taper to a narrower neck near their junction with the tail. In contrast, myosin heads that lack the regulatory light chains appear more globular. The neck region is no longer visible: the rounded heads appear directly attached to the tail or there is an apparent gap between the head and the tail. Two preparations of myosin subfragment-1 that differ in light chain content show a similar difference in appearance. Fab fragments of antibodies specific for the light chains bind to the myosin heads and can also be visualized in the electron microscope using rotary shadowing. Both Fab fragments specific for the regulatory light chains and Fab fragments specific for the essential light chains bind preferentially to intact scallop myosin in the narrow region of the myosin head near its junction with the tail.
D000818:Animals; D002118:Calcium; D004492:Edetic Acid; D004591:Electrophoresis, Polyacrylamide Gel; D007140:Immunoglobulin Fab Fragments / Q000276:immunology; D008274:Magnesium; D008854:Microscopy, Electron; D008974:Mollusca; D009218:Myosins / Q000276:immunology; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation
D007140:Immunoglobulin Fab Fragments; D010446:Peptide Fragments; D004492:Edetic Acid; D009218:Myosins; D008274:Magnesium; D002118:Calcium