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Enhancement of in vitro antibody responses by human serum proteins cleaved by trypsin
Tryptic cleavage of human serum proteins remarkably enhanced in vitro plaque-forming cell (PFC) responses of mouse spleen cells primed with sheep erythrocytes (SE). Moreover, trypsin cleaved proteins could mimic the activity of T-cells in immune responses of SE-primed B cells. Eluted with 6 M guanidine-HCl on a Sepharose 6B-CL Column, the activity was found in the fraction corresponding to the molecular weight greater than 100,000. The results suggest that tryptic cleavage of human serum proteins produced a factor(s) that resembled the T-cell augmentation of B-cell immune responses.
Tryptic cleavage of human serum proteins remarkably enhanced in vitro plaque-forming cell (PFC) responses of mouse spleen cells primed with sheep erythrocytes (SE). Moreover, trypsin cleaved proteins could mimic the activity of T-cells in immune responses of SE-primed B cells. Eluted with 6 M guanidine-HCl on a Sepharose 6B-CL Column, the activity was found in the fraction corresponding to the molecular weight greater than 100,000. The results suggest that tryptic cleavage of human serum proteins produced a factor(s) that resembled the T-cell augmentation of B-cell immune responses.