Heterogeneity of 27,000 dalton-light chain of cardiac ventricular myosin.
Electrophoretic analysis on sodium pyrophosphate gels of myosin light chain 1 (LC-1; 27,000 daltons) from rabbit ventricular heart muscle revealed the presence of two distinct components named LC-1a (10%) and LC-1b (90%). After thyroxine administration, a shift toward LC-1a (45%) was observed. Canine cardiac ventricular light chain 1 (27,000 daltons) had equal amounts of LC-1a' (50%) and LC-1b' (50%), which corresponded to LC-1a and LC-1b of rabbit heart, respectively. However, heterogeneity of light chain 2 (20,000 daltons) was not observed. It is concluded that cardiac ventricular myosin has two heterogeneous 27,000 dalton-light chains and that the proportion of these proteins varies according to the thyroid status and animal species.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006321:Heart / Q000187:drug effects; D006352:Heart Ventricles / Q000032:analysis; D008297:Male; D009206:Myocardium / Q000032:analysis*; D009218:Myosins / Q000302:isolation & purification* / Q000378:metabolism; D011817:Rabbits; D013974:Thyroxine / Q000494:pharmacology
D009218:Myosins; D013974:Thyroxine