Isolation and characterization of myosin from subjects with asymmetric septal hypertrophy.
Human cardiac myosin isolated from operatively obtained samples of ventricular septum and left ventricular free wall of subjects with asymmetric septal hypertrophy (ASH) was compared, with respect to structural and enzymatic properties, to myosin isolated from hearts of subjects without heart disease. The following parameters were studied: (1) activation of myosin ATPase activity by K+-EDTA and Ca2+, (2) molecular weight of the heavy and light chains of myosin as determined by electrophoretic migration in polyacrylamide-sodium dodecyl sulfate (SDS) gels and (3) ability to form bipolar aggregates at low ionic strength, as examined by electron microscopy. No difference was present in any of these parameters between human cardiac myosin from subjects with ASH and from subjects without heart disease. Thus, the genetic defect present in subjects with ASH is not expressed in the particular structural and functional characteristics of myosin evaluated in this study.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D000328:Adult; D000368:Aged; D006332:Cardiomegaly / Q000201:enzymology / Q000378:metabolism*; D004492:Edetic Acid / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005260:Female; D006346:Heart Septum / Q000032:analysis* / Q000201:enzymology; D006352:Heart Ventricles / Q000201:enzymology; D006801:Humans; D008297:Male; D008875:Middle Aged; D009218:Myosins / Q000302:isolation & purification*; D011188:Potassium / Q000494:pharmacology
D004492:Edetic Acid; D000251:Adenosine Triphosphatases; D009218:Myosins; D011188:Potassium