Myosin Isozymes in Vertebrate Smooth Muscles
(1987)
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- Authors
Maréchal, Georges 
- Abstract
- (en) Electrophoreses of smooth muscle extracts (chicken gizzard; guinea-pig taenia coli; canine and human stomach and colon) in non-dissociating pyrophosphate gels yield 1 to 4 zones according to the composition of the extracting solution or the temperature of the electrophoretic runs. We called the 3 zones: G2, GI and G0, by order of increasing mobilities. Reelectrophoresis on SDS-12% PAA gels show two light chains (17 and 20 kDa) for G2, GI and G0, on SDS-6% PAA: heavy chains of 230 kDa for G2, 200 kDa for G0 and a mixture of the two for Gl. Antifilamin added to the extract at an approximate molar ratio of 4/1 depresses G2 by 80 to 100% and Cl by 50%. Anti-smooth muscle LMM binds to Western blots of G2, Cl and G0. These results indicate that contrary to our earlier proposal, [Beckers-Bleukx & Maréchal, Eur. J. Biochem. 152, 207-11 (1985)1 G2 and G1 probably do not contain myosin isoforms but myosin-filamin complexes of different molar ratio (1/4 and 1/1 respectively) whilst G0 contains myosin but no filamin.
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Citations
Beckers-Bleukx, G., & Maréchal, G. (1987). Myosin Isozymes in Vertebrate Smooth Muscles. Journal of Muscle Research and Cell Motility, 8(1), 76. (Original work published 1987)