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R J BROWN

Publications and source records attributed to R J BROWN.

16 recordsLinked to original sources
PubMed1962

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

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.

Animals↗
PubMed1962

Adsorption of influenza A virus by Aerobacter aerogenes spheroplasts.

Brown, Ronald J. (University of Kansas, Lawrence), Albert A. Benedict, and Nancy Armstrong. Adsorption of influenza A virus by Aerobacter aerogenes spheroplasts. J. Bacteriol. 83:1124-1130. 1962.-Aerobacter aerogenes spheroplasts adsorbed virus at a greater rate than whole A. aerogenes cells or cell-wall preparations. The largest fragments of sonic-disrupted spheroplasts were responsible for adsorption. Adsorption was characterized by rapid disappearance of viral hemagglutinin in about 8 min, elution of hemagglutinin, and followed again by complete adsorption of hemagglutinin. Viral activity was not recovered from spheroplasts after the final adsorption phase. Spheroplasts treated with heat, dilute periodate, or formaldehyde did not adsorb virus, and treatment of spheroplasts with receptor-destroying enzyme resulted in delayed adsorption.

Adsorption↗