Crystallization and Physical Characterization of Porcine Myoglobin

Porcine myoglobin was isolated by fractionation with ammonium sulfate and crystallized with 3.8 M phosphate buffer.

Chromatography of the porcine crystalline myoglobin on a molecular-sieve column gave a single elution band, which agreed well with that of horse myoglobin.

By ultracentrifugal analysis, the sedimentation constant (s_20,w), was found to be 1.96 S.

The iron content of the myoglobin was 0.324%. This value corresponds to the minimal molecular weight of 17,200.

Absorption curves and millimolar extinction coefficients of the porcine myoglobin in several derivatives, namely, reduced (RMb), met (MMb), carboxy (MbCO) and cyanment (MMbCN) forms were examined in the visible region. The spectral characteristics of the porcine myoglobin derivatives were in good agreement with those of horse myoglobin,

Three components were detected for the porcine myoglobin by starch gel electrophoresis, and each of them had higher migration velocity than those of horse myoglobin.