@entity2823 ( @entity2822 )-labeled albumin was used as a substrate to further characterize the digestion of host blood proteins by adult @entity5167 . Isolated @entity5167 intestine degraded @entity2823 -albumin; degradation was completely inhibited by E-64, a specific inhibitor of @entity462 proteases. The in vitro uptake and degradation of @entity2823 -albumin by parasites was also evaluated. Uptake of fluorescence was demonstrated; greater than 50% of the fluorescence was associated with degraded @entity2823 -albumin. However, both the uptake and degradation of @entity2823 -albumin were reduced by about 85%. Additionally, when parasites were incubated in the presence of specific inhibitors of @entity462 proteases, degradation of @entity2823 -albumin was shown to occur rapidly in the media during in vitro incubation. This degradation was blocked completely by the presence of @entity462 protease inhibitors. These results indicate that the rapid extracorporeal digestion of @entity2823 -albumin (mediated by secreted @entity462 proteases) produce relatively high concentrations of low molecular weight @entity2823 -labeled fragments and alters the kinetics of uptake of fluorescence by the parasite. These fragments rather than @entity2823 -albumin are rapidly taken up by the parasites. Thus in vitro demonstration of a definitive role for the @entity462 proteases as intestinal digestive enzymes in @entity5167 is compromised by the enzyme's extracorporeal activity. This extracorporeal @entity462 protease activity may represent the enzyme's predominant activity.

The in vitro uptake of albumin by adult XXXX is altered by extracorporeal digestion.

@entity462 :: ('MESH:D003545', 'Chemical') :: ['cysteine'] @entity2823 :: ('MESH:D016650', 'Chemical') :: ['FITC'] @entity2822 :: ('CHEBI:37926', 'Chemical') :: ['fluorescein isothiocyanate'] @entity5167 :: ('6289', 'Species') :: ['H. contortus', 'Haemonchus contortus']
@entity5167 :: (6289,Species) :: ['Haemonchus contortus']
