Identical myoglobin is present in both skeletal and smooth muscles of chicken.

Chicken gizzard has been considered to be an exceptional organ of smooth musculature in which a myoglobin is present. Since the characterization of the gizzard myoglobin has to date, been very incomplete, we studied the structures and functions in detail. The main component, which constituted roughly 90% of the protein, isolated by chromatofocusing, was homogeneous by electrophoretic and ultracentrifugal analyses. The molecular weight was consistently 1.8 X 10(4) by equilibrium sedimentation and iron analysis, and the isoelectric point was 7.8. Spectroscopic properties of the oxy-, carboxy- and deoxy-derivatives were typical of myoglobin. The oxygenation equilibria were also typical of myoglobin, showing neither homotropic nor heterotropic allosteric interactions, and the temperature-dependence (delta H0) was estimated as -16.6 kcal/mol. All these characteristics of the gizzard myoglobin were identical with those of the protein from the skeletal muscles. The amino acid composition and peptide mapping results also concluded that identical myoglobin was present in the gizzard, skeletal and probably cardiac muscles.