Structural differences between atrial and ventricular myosins from normal human hearts.
Comparisons were made between myosins isolated from the right and left ventricles and the atria of normal human hearts. Parameters examined included electrophoretic mobilities of native molecules, K+ and Ca2+ dependent enzymatic activities, light chain composition, peptide patterns from partial proteolytic digests of entire heavy chains or rods, and maps of complete digests of specific 21 and 25 kilodalton heavy chain fragments. Human ventricular and atrial myosins differ in all parameters except in the charge of molecules. Structural differences between cardiac myosins derived from the two sources were apparent in both the head and tail portions of the heavy chains. With respect to the above parameters no differences were found between myosins from left and right human ventricles.
D000251:Adenosine Triphosphatases / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006325:Heart Atria / Q000032:analysis; D006352:Heart Ventricles / Q000032:analysis; D006801:Humans; D009206:Myocardium / Q000032:analysis* / Q000201:enzymology; D015879:Myosin Subfragments; D009218:Myosins / Q000302:isolation & purification*; D009928:Organ Specificity; D010446:Peptide Fragments / Q000032:analysis / Q000302:isolation & purification
D015879:Myosin Subfragments; D010446:Peptide Fragments; D000251:Adenosine Triphosphatases; D009218:Myosins