Abnormal Spectrophotometric Absorption Spectrums of Myoglobin in Two Forms of Progressive Muscular Dystrophy

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Abstract
AFTER the discovery by Pauling et al.1 of an abnormal molecular form of hemoglobin in patients with sickle-cell anemia and the subsequent demonstration of many similarly abnormal hemoglobins, speculation arose concerning the possibility of comparable alterations of the molecular structure of myoglobin in certain primary diseases of muscle.2 , 3 In a search for such abnormalities, Perkoff and his associates3 , 4 studied myoglobin isolated from a patient with the myotonic form of muscular dystrophy and reported its spectrophotometric absorption spectrum and electrophoretic mobility to be normal. They were not able to demonstrate abnormalities in crude extracts of myoglobin prepared from cardiac muscle from . . .