Relationship between the synthesis rates and mRNA levels of the α and β cardiac myosin heavy chains in normal and thyrotoxic rabbits

1983 ◽  
pp. 39-45 ◽  
Author(s):  
A. W. Everett ◽  
A. M. Sinha ◽  
M. Rabinowitz ◽  
Radovan Zak
Keyword(s):  
Mrna Levels ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Heavy Chains

Variations in the Relative mRNA Levels of Actins and Myosin Heavy Chains do not Produce Corresponding Differences in their Proteins in the Adult Human Heart

1997 ◽  
Vol 29 (3) ◽  
pp. 895-905 ◽  
Author(s):  
Joëlle V.F. Coumans ◽  
Thomas Yeoh ◽  
Reginald K. Seeto ◽  
Anne Keogh ◽  
Karen Brennan ◽  
...  
Keyword(s):  
Human Heart ◽  
Mrna Levels ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Adult Human

Cardiac myosin heavy chains in mice treated with NG-nitro-l-arginine methyl ester and thyroxine

2013 ◽  
Vol 23 (5) ◽  
pp. 1639-1644 ◽  
Author(s):  
Mukhallad A. M. Mohammad ◽  
Muhanad S. Abdelwahab ◽  
Mohamad M. J. Mohamad ◽  
Othman El shboul ◽  
Waleed R. Ezzat
Keyword(s):  
Methyl Ester ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Heavy Chains

Cardiac Myosin Heavy Chains

2019 ◽  
Vol 8 (1) ◽  
pp. 1-7
Author(s):  
Muhanad S. Abdelwahab ◽  
Mukhallad Am. Mohamemed ◽  
Abdelwahab Hassan Mohamed ◽  
Mansour Abdelgader Bellal ◽  
Mazin S. Abdalla Mohamed
Keyword(s):  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Heavy Chains

scholarly journals Visualization of cardiac ventricular myosin heavy chain homodimers and heterodimers by monoclonal antibody epitope mapping.

1987 ◽  
Vol 105 (6) ◽  
pp. 3031-3037 ◽  
Author(s):  
C A Dechesne ◽  
P Bouvagnet ◽  
D Walzthöny ◽  
J J Léger
Keyword(s):  
Heavy Chain ◽  
Binding Sites ◽  
Epitope Mapping ◽  
Myosin Molecule ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Heavy Chains ◽  
Ventricular Myosin ◽  
Alpha Beta ◽  
Myosin Rod

Two mAbs, one specific for cardiac alpha-myosin heavy chains (MHC) and the other specific for cardiac beta-MHC, were used to investigate the heavy-chain dimeric organization of rat cardiac ventricular myosin. Epitopes of the two mAbs were mapped on the myosin molecule by electron microscopy of rotary shadowed mAb-myosin complexes. mAbs were clearly identifiable by the different locations of their binding sites on the myosin rod. Thus, myosin molecules could be directly discriminated according to their alpha-or beta-MHC content. alpha alpha-MHC and beta beta-MHC homodimers were visualized in complexes consisting of two molecules of the same mAb bound to one myosin molecule. By simultaneously using the alpha-MHC-specific mAb and the beta-MHC-specific mAb, alpha beta-MHC heterodimers were visualized in complexes formed by one molecule of each of the two mAbs bound to one myosin molecule. Proportions of alpha alpha-and beta beta-MHC homodimers and alpha beta-MHC heterodimers were estimated from quantifications of mAb-myosin complexes and compared with the proportions given by electrophoreses under nondenaturing conditions. This visualization of cardiac myosin molecules clearly demonstrates the arrangement of alpha- and beta-MHC in alpha alpha-MHC homodimers, beta beta-MHC homodimers, and alpha beta-MHC heterodimers, as initially proposed by Hoh, J. F. Y., G. P. S. Yeoh, M. A. W. Thomas, and L. Higginbottom (1979).

Sign in / Sign up

Export Citation Format

Share Document