Abstract
Summary and Conclusion The nature of the enzymatic action on human red blood cells by weak solutions of certain proteolytic enzymes was studied,particularly with reference to the properties acquired which allow them to be agglutinated by homologous “incomplete” anti-Rh antibodies in saline media. The optimal conditions with respect to trypsin concentration, time, pH, and temperature for the treatment of red cells so that they take on these properties has been discussed. It would appear from the present data that this enzyme modification involves an alteration of the red cell surface to produce both a diminished cell “suspension stability” and a “rearrangement” or “uncovering” of portions of the antigenic moiety. Trypsin-modified red cells have been employed as extremely sensitive indicators for the detection of anti-11h and other blood group antibodies, both complete and incomplete. Agglutination reactions with such cells are specific, easily read,immediate,and unlikely to show failure of agglutination because of serum prozones.
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