Globulin Fractions Separated From Antipertussis Rabbit Serum

Abstract

Globulins of antipertussis and of normal rabbit serum were fractionated by diethylaminoethyl cellulose (DEAE-cellulose) chromatography. Concentration of antipertussis globulins resulted in two elution areas-first, by 0.05M of tromethamine (tris buffer [tris (hydroxymethyl) aminomethane]) at a pH determination of 8.2, followed by sodium chloride gradient. That is, following immunization, rabbits produced active antipertussis IgG (7Sγ) globulins of two different charges. Comparing antipertussis and normal globulins, their protein concentrations following NaCI gradient elution were similar. However, with tromethamine, the high protein-concentration observed for antipertussis globulins was lacking for normal globulins. All active antipertussis globulins had both serologic and mouse-protective activities. Separation of the two activities was not demonstrated. It is suggested that studies of antipertussis globulins prepared in response to purified antigens could add importantly to existing knowledge of pertussis antigens. At the same time, this approach might contribute to studies on the mechanism of antibody formation.