Electrophoretic properties of the globins of bovine hemoglobins A and B

Abstract

The globins isolated from bovine hemoglobins A and B were investigated by moving-boundary electrophoresis at pH's 2.4, 4.25, 5.4, and 10.7. At the intermediate pH levels, both globins had two components, the relative proportions of which changed in favor of the slow component as the pH was decreased. At pH 2.4, both globins had three components in the same relative proportions. The mobilities of corresponding components were essentially the same for the two globins at the three lower pH levels. At pH 10.7, both globins had two components. The slower component had the same mobility in the two globins, but the mobility of the faster components differed significantly. No differences between crude and renatured, or between denatured and renatured globin fractions were observed. The two primary components of globins A and B were isolated by continuous flow paper electrophoresis. At pH 4.25, both components of both globins appeared to be electrophoretically homogeneous, but at pH 2.4 both fractions of both globins dissociated into subunits. The newly dissociated component had the same mobility whatever its source, but the amount depended on whether it came from the fast or slow primary component.