Several antisera human erythrocyte glucose 6-phosphate dehydrogenase (G6PD, type B) have been raised in rabbits and used for the characterization of genetic variants of this enzyme protein. Use of the anti-G6PD antisera for estimating the specific activity of G6PD variants has recently been criticized and shown to be inadequate to this purpose. Moreover, both the specificity and strength of conventional antisera are not satisfactory enough to allow a precise characterization of G6PD variants associated with severe deficiency of activity. In an attempts to overcome thes limitations, we used cell fusion techniques to obtain anti-G6PD antibody-secreting hybridomas. By this approach, a number of antibodies directed to human G6PD were isolated after fusion of an 8-azaguanine-resistant mouse myeloma line with splenocytes from a mouse hyperimmunized with G6PD.
Monoclonal antibodies to human erythrocyte glucose 6-phosphate dehydrogenase
FRASCIO, MARCO;BENATTI, UMBERTO
1980-01-01
Abstract
Several antisera human erythrocyte glucose 6-phosphate dehydrogenase (G6PD, type B) have been raised in rabbits and used for the characterization of genetic variants of this enzyme protein. Use of the anti-G6PD antisera for estimating the specific activity of G6PD variants has recently been criticized and shown to be inadequate to this purpose. Moreover, both the specificity and strength of conventional antisera are not satisfactory enough to allow a precise characterization of G6PD variants associated with severe deficiency of activity. In an attempts to overcome thes limitations, we used cell fusion techniques to obtain anti-G6PD antibody-secreting hybridomas. By this approach, a number of antibodies directed to human G6PD were isolated after fusion of an 8-azaguanine-resistant mouse myeloma line with splenocytes from a mouse hyperimmunized with G6PD.
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
