Abstract
Myosin extracted from ventricular muscle of the urodelan amphibian Pleurodeles waltlii was analyzed in comparison with myosin extracted from skeletal muscles by native, one-dimensional SDS gel electrophoresis and two-dimensional gel electrophoresis. Two myosin isoforms were detected in ventricular muscle using pyrophosphate gel electrophoresis. These isomyosins contained two types of light chain subunits, LClv and LC2v. Two-dimensional gel electrophoresis showed that LClv comigrated with the slow light chain LCls, whereas LC2v was characterized by a specific mobility, distinct from LC2s and LC2f. Diaphragm muscle was characterized by the coexistence of larval and adult myosin isoforms.
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