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

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

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).

scholarly journals Epitopes of streptococcal M proteins shared with cardiac myosin.

1985 ◽  
Vol 162 (2) ◽  
pp. 583-591 ◽  
Author(s):  
J B Dale ◽  
E H Beachey
Keyword(s):  
Acute Rheumatic Fever ◽  
M Protein ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Myosin Heavy Chains ◽  
Cardiac Myosin ◽  
Poststreptococcal Glomerulonephritis ◽  
Heavy Chains ◽  
M Proteins ◽  
Group A

We present evidence that M proteins from three different serotypes of group A streptococci share epitopes with cardiac myosin. Rabbit antisera evoked by a purified fragment of type 5 M protein crossreacted with myosin, but not alpha-tropomyosin, actin, or myosin light chains. In enzyme-linked immunosorbent assays, the myosin-crossreactive antibodies were totally inhibited by type 5 M protein and partially inhibited by types 6 and 19 M proteins. The affinity-purified myosin antibodies opsonized type 5 streptococci, indicating that they were directed against protective M protein epitopes on the surface of the organisms. Immunoblot analyses demonstrated the binding of the crossreactive antibodies to myosin heavy chains. Sera from patients with acute rheumatic fever showed significantly stronger reactions with myosin than did sera from their siblings, hospitalized controls, or patients with poststreptococcal glomerulonephritis.

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