Ascaris suum: biosynthesis and isoinhibitor profile of chymotrypsin/elastase isoinhibitors.
Chymotrypsin/elastase isoinhibitors were radiolabeled when live, adult Ascaris suum were incubated in tissue culture medium (NCTC-135) supplemented with L-[35S]cysteine. This is the first demonstration that the synthesis of these proteins occurs in A. suum; the isoinhibitors are not host products utilized by the parasite against its host. Of five chymotrypsin/elastase isoinhibitors demonstrable in A. suum, only isoinhibitors 1, 4, and 5 were found in each worm. The amino acid sequences of these three isoinhibitors indicate that they are gene products and are not obtained by modification after translation. The two inhibitors that are not observed could arise by limited proteolysis. The same chymotrypsin/elastase isoinhibitor profile present in each nematode eliminates any speculation that the multiple forms arise from an adaptation between A. suum and its host. A new chymotrypsin/elastase isoinhibitor nomenclature is proposed, so that isoinhibitor 1 is now Isoinhibitor A, and isoinhibitors 4 and 5 are now Isoinhibitors B and C, respectively.
D000818:Animals; D001200:Ascaris / Q000378:metabolism*; D002846:Chromatography, Affinity; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008297:Male; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D013552:Swine / Q000469:parasitology
D002918:Chymotrypsin; D010196:Pancreatic Elastase