Fluorescence intensity and UV absorption changes accompanying dissociation and association of regulatory light chain of scallop adductor myosin.
Dissociation and association of regulatory light chains of scallop myosin were found to be accompanied by changes in the fluorescence intensity and in the UV absorption spectrum. The changes in the two optical properties of scallop myosin and the dissociation and association of regulatory light chains were studied as a function of the magnesium and calcium concentrations. The results thus obtained suggested that there are two different types of attachment between regulatory light chains and "desensitized" myosin; one type is a calcium-specific attachment, and the other type of attachment can be mediated by either calcium or magnesium ions. These changes in the optical properties of scallop myosin were distinguishable from those induced by Mg-ATP; for example, with "desensitized" scallop myosin, the former changes were not observed but the latter were.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004492:Edetic Acid / Q000494:pharmacology; D007700:Kinetics; D046911:Macromolecular Substances; D008274:Magnesium / Q000494:pharmacology; D008974:Mollusca / Q000378:metabolism*; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet
D046911:Macromolecular Substances; D000255:Adenosine Triphosphate; D004492:Edetic Acid; D009218:Myosins; D008274:Magnesium; D002118:Calcium