Characterization of myosin from patients with asymmetric septal hypertrophy.
Human cardiac myosin isolated from operatively obtained samples of ventricular septum and left ventricular free wall of patients with asymmetric septal hypertrophy (ASH) was compared, with respect to structural and enzymatic properties, to myosin isolated from hearts of patients 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 SDS-polyacrylamide 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 patients with ASH and from patients without heart disease. Thus, the genetic defect present in patients with ASH is not expressed in the particular structural and functional characteristics of myosin evaluated in this study.
D000205:Actomyosin / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000328:Adult; D000368:Aged; D009202:Cardiomyopathies / Q000378:metabolism*; D005260:Female; D006801:Humans; D046911:Macromolecular Substances; D008970:Molecular Weight; D009206:Myocardium / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*
D046911:Macromolecular Substances; D000205:Actomyosin; D000251:Adenosine Triphosphatases; D009218:Myosins