Physicochemical Studies on the Light Chains of Myosin

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Abstract
The myosin light chain of intermediate molecular weight, LMP-II, undergoes a marked reduction in its electrophoretic migration rate in response to Ca2+, compared to the other light chains run under the same conditions. Other divalent, but not monovalent, cations had a similar effect; These results support earlier tryptophan fluorescence measurements showing that LMP-II binds Ca2+ ions. The possible role played by these light chains—which are not required for the ATPase [EC 3.6.1.3] activity of myosin, and which have therefore been considered as nonessential—s discussed.

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