Myosin isoforms and their light chains from the ventricular muscle of the urodelan amphibian Pleurodeles waltlii: comparison with myosin from skeletal muscles.
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, LC1v and LC2v. Two-dimensional gel electrophoresis showed that LC1v comigrated with the slow light chain LC1s, 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.
Launay
T
T
Laboratoire de Biologie du Développement, URA CNRS 1188, Université René Descartes, Paris, France.
Gallien
C L
CL
Chanoine
C
C
D000367:Age Factors; D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006352:Heart Ventricles / Q000737:chemistry*; D007527:Isoenzymes; D018482:Muscle, Skeletal / Q000737:chemistry*; D018994:Myosin Light Chains / Q000737:chemistry; D009218:Myosins / Q000737:chemistry*; D010999:Pleurodeles / Q000502:physiology*
D007527:Isoenzymes; D018994:Myosin Light Chains; D009218:Myosins