Abstract
Summary
Purified duck myoglobin was prepared by ammonium sulfate precipitation and ion-exchange chromatography. Its sedimentation constant was estimated to be approximately 1.75. A specific precipitating antiserum to duck myoglobin was prepared in rabbits. This antiserum did not form precipitates with duck plasma, hemoglobin, liver extract or with components of crude muscle extracts other than myoglobin. No immunologic differences were detectable between duck cardiac or skeletal muscle myoglobin, and none were noted between myoglobins of goose, duck, or chicken present in muscle extracts. Chicken pectoral muscle lacked myoglobin. Precipitin data suggest that three regions on the duck myoglobin molecule act as combining sites or determinants for the rabbit serum. The myoglobin content of several avian muscles was measured immunologically. Skeletal muscle of newly hatched ducklings was deficient in myoglobin content, while cardiac muscle of these immature birds contained almost one-half the adult amount 2 days after hatching, and reached nearly adult levels at 8 days after hatching.
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