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. 1962 Jan 1;115(1):195-208.
doi: 10.1084/jem.115.1.195.

Physical properties of antibody to bovine serum albumin as demonstrated by hemagglutination

A A BENEDICT, R J BROWN, R AYENGAR

Physical properties of antibody to bovine serum albumin as demonstrated by hemagglutination

A A BENEDICT et al. J Exp Med. .

Abstract

Rabbit antibovine serum albumin antisera were fractionated by zone electrophoresis on starch, zone ultracentrifugation in sucrose density gradients, and diethylaminoethyl-cellulose chromatography, and were assayed by the passive HA technique. Antisera had at least two antibodies: one associated with a fraction characterized as a gamma-2 globulin with a sedimentation rate of 7.3S and low anionic binding (fraction I), and one associated with a fraction characterized as a gamma-1 globulin (or beta-globulin) with a sedimentation rate of 20.4S and high anionic binding (fraction IV). The HA titers of fractions I and IV of early sera were approximately equal. On prolonged antigenic stimulation fraction IV agglutinin decreased in concentration and the relative concentration of fraction I agglutinin increased. Chromatographic analysis of hyper-immune sera yielded 2 additional HA fractions with intermediate anionic binding. These results indicated that rabbits synthesize anti-BSA antibodies similar to rabbit anti-cellular antibodies. Rabbit anti-BSA precipitin migrated mainly as a gamma-2 globulin and the agglutinin migrated with gamma- and beta-globulins. The evidence suggested that the HA method might measure antibody not measured by the quantitative precipitin technique.

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