Abstract
Pyrophosphate gel electrophoresis has been established as a sensitive and reliable method of resolving myosin isozymes. The existence of 3 isozymes of vertebrate fast myosin differing in their alkali light chain distribution is well documented. In order of increasing mobility they represent the (LCr)a(LC&, (LCr)(LC&(LCa) and (LC&(LC& species [1,2,3]. However, in rat ventricular myosin, where only one light chain is analogous to the alkali light chains of fast skeletal myosin, the isozymes differ with respect to the iso-forms of 2 distinct heavy chains [4,5]. Fast skeletal myosin isozymes differ in the heavy chain [6-91. In case of rabbit slow myosin no isozymes were distinguishable on pyrophosphate gel [IO]. The existence of 2 different light chains (LCI,,LCIb) analogous to the alkali light chains of fast myosin [ 111, and as reported here, the existence of 2 forms of slow subfragment-l (S-l) separated in pyrophosphate gel suggests the presence of the isozymes analogous to the fast myosin isozymes. On the basis of analysis in pyrophosphate gels of single fibers, some of which contain predominantly either LC,, or LCrb, there are at least 2 isozymes of rabbit slow myosin namely, (LC&(LC& and (LCrb)z(LC2)2 horndims.
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