Electrophoretic Separation of Ventricular Myosin Isoenzymes Using a Native Polyacrylamide Minigel System

2003 ◽  
Vol 38 (1) ◽  
pp. 33-40 ◽  
Author(s):  
S. C. Garcia Pomblum ◽  
V. J. Pomblum ◽  
E. Gams ◽  
P. J. Reiser ◽  
J. D. Schipke
Keyword(s):  
Electrophoretic Separation ◽  
Myosin Isoenzymes ◽  
Ventricular Myosin

Developmental changes in ventricular myosin isoenzymes of the tammar wallaby

2007 ◽  
Vol 177 (6) ◽  
pp. 701-705 ◽  
Author(s):  
Yoonah Kim ◽  
Christine A. Lucas ◽  
Wendy W. H. Zhong ◽  
Joseph F. Y. Hoh
Keyword(s):  
Tammar Wallaby ◽  
Developmental Changes ◽  
Myosin Isoenzymes ◽  
Ventricular Myosin

Swimming exercise, thyroid state, and the distribution of myosin isoenzymes in rat heart

1983 ◽  
Vol 245 (5) ◽  
pp. H713-H720 ◽  
Author(s):  
E. D. Pagani ◽  
R. J. Solaro
Keyword(s):  
Thyroid Hormone ◽  
Atpase Activity ◽  
Gel Electrophoresis ◽  
Male Rats ◽  
Swimming Exercise ◽  
Cardiac Myosin ◽  
Thyroid State ◽  
Sedentary Group ◽  
Myosin Isoenzymes ◽  
Ventricular Myosin

We tested whether changes in cardiac myosin ATPase activity induced by swimming exercise in male rats are due to a redistribution of existing isoenzymic forms of ventricular myosin. The isoenzymic profiles were analyzed by nondissociating gel electrophoresis of ventricular samples and compared with ATPase activities of myofibrils prepared from the same ventricle. Myofibrils prepared from hearts of rats in the control sedentary group or from hearts of rats in the groups of 8- or 12-wk swimmers had the same actomyosin Mg2+-ATPase activities measured between pCa 8 and 5. However, the myosin Ca2+-ATPase activity of myofibrils prepared from hearts of 8- or 12-wk swimmers was 20% higher than the activity of control preparations. This increase in activity was in proportion to an increase in the relative amount of V1, the myosin isoenzyme with the highest Ca2+-ATPase activity. Thyroidectomized rats, whose hearts had no detectable V1, were also subjected to the swimming program. In the case of the hypothyroid rats, myofibrillar preparations from controls and 8- or 12-wk swimmers had the same actomyosin Mg2+-ATPase activity, myosin Ca2+-ATPase activity, and the same isoenzyme profiles. Co-electrophoresis of ventricular samples from the euthyroid and hypothyroid controls and swimmers showed no evidence for new variants of myosin. We conclude that the increase in myosin Ca2+-ATPase activity in the ventricles of euthyroid swimmers is due to a redistribution of existing isoforms of myosin and that the redistribution process may require thyroid hormone for its expression.

Effects of regression of cardiac hypertrophy on myocardial contractility and ventricular myosin isoenzymes

1992 ◽  
Vol 118 (1) ◽  
pp. 99-103 ◽  
Author(s):  
Takaaki Iwai ◽  
Nobuakira Takeda ◽  
Masahito Tuchiya ◽  
Tohru Arino ◽  
Akira Tanamura ◽  
...  
Keyword(s):  
Cardiac Hypertrophy ◽  
Myocardial Contractility ◽  
Myosin Isoenzymes ◽  
Ventricular Myosin ◽  
Regression Of Cardiac Hypertrophy

scholarly journals THE PAPER ELECTROPHORETIC SEPARATION OF PHOSPHATIDES

1958 ◽  
Vol 230 (2) ◽  
pp. 621-624
Author(s):  
Herbert Zipper ◽  
Morton D. Glantz
Keyword(s):  
Electrophoretic Separation
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