Tryptic digestion of native small-intestinal sucrase - isomaltase complex: isolation of the sucrase subunit.
Limited tryptic digestion of native sucrase - isomaltase complex produced a more rapid destruction of isomaltase activity than sucrase activity. It was possible to isolate a partially fragmented sucrase subunits in high yields with a specific activity twice that of the native complex. Amino acid and carbohydrate analyses are reported and compared with the results obtained for sucrase - isomaltase complex and isomaltase subunit obtained by a different method.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002241:Carbohydrates / Q000032:analysis; D005959:Glucosidases / Q000302:isolation & purification / Q000378:metabolism; D007421:Intestine, Small / Q000201:enzymology*; D007700:Kinetics; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism; D011817:Rabbits; D013393:Sucrase / Q000302:isolation & purification / Q000378:metabolism; D014357:Trypsin
D000596:Amino Acids; D002241:Carbohydrates; D009097:Multienzyme Complexes; D005959:Glucosidases; D013393:Sucrase; D014357:Trypsin