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F KARUSH

Publications and source records attributed to F KARUSH.

13 recordsLinked to original sources

VALENCE AND AFFINITY OF EQUINE NONPRECIPITATING ANTIBODY TO A HAPTENIC GROUP.

A nonprecipitable antibody to a haptenic group has been purified from equine serum. It is a 7S beta2delta immunoglobulin with high affinity for the specific hapten and two binding sites per antibody molecule. These results rule out univalence and low affinity as explanations of the nonprecipitability of this antibody.

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EQUINE ANTIHAPTEN ANTIBODY. I. 7S BETA-2A- AND 1OS GAMMA-1- GLOBULIN COMPONENTS OF PURIFIED ANTI-BETA-LACTOSIDE ANTIBODY.

Anti-p-azophenyl-beta-lactoside (Lac) antibody has been isolated from equine antiserum by specific precipitation with Lac-HSA (human serum albumin) and Lac-Hy (hemocyanin). Antibody was separated from antigen by chromatography on DEAE cellulose and zone electrophoresis in solvents containing lactose. Six antigenically distinct immunoglobulins have been identified in purified equine anti-Lac antibody: 7S beta(2A)-globulin, 19S gamma-globulin, a 10S gamma(1) globulin, and three antigenically distinct 7S gamma-globulins. The specific hapten-binding activity of the 7S beta(2A)-antibody and of the 10S gamma(1)-antibody has been demonstrated by equilibrium dialysis and by analytical ultracentrifugation using a combination of schlieren and absorption optics. The 10S gamma(1)-globulin antibody may be representative of a hitherto undescribed class of immunoglobulins.

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