Precipitin reactions of anti-human myoglobin serum with several human and animal muscle extracts.

Abstract

Myoglobin content of several human muscles was determined immunologically. The content of cardiac and skeletal muscle was similar. There was no antigenic difference noted between cardiac and skeletal muscle myoglobin. Uterine smooth muscle contained no myoglobin. Details of the precipitin reaction between human myoglobin and its antiserum are presented. There may be approximately three regions on the human myoglobin molecule which acted as antigenic sites in a rabbit. Several animal muscle extracts cross-reacted with the anti-human myoglobin. All primate skeletal muscle samples tested were equally potent, while beef, rodent and chicken thigh muscle extracts were poorer cross-reactors. It is postulated that these differences were due to differences in the myoglobin molecules of these species. Chicken breast muscle did not cross-react, and appeared to be deficient in myoglobin.