EFFECT OF PH AND COLUMN SIZE ON CM-CELLULOSE CHROMATOGRAPHY OF BOVINE MYOGLOBIN

The several fractions obtained by chromatography of bovine myoglobin on CM-cellulose can be explained partially in terms of a pH anomaly. Adsorption of myoglobin on CM-cellulose causes the pH to rise, and unadsorbed myoglobin moves down the column with the solvent front. This fast-moving fraction (FMF) contains the several fractions that make myoglobin microheterogeneous, and the FMF is gradually adsorbed as it moves down the column. Subsequent elution of myoglobin leads to distinct fractions, which are heterogeneous on gel electrophoresis. This explanation of the chromatographic behavior of myoglobin, along with a suggested nomenclature for the chromatographic fractions, should remove some of the confusion concerning the microheterogeneity of myoglobin. © 1968.