A hydrophobic form of the small-intestinal sucrase-isomaltase complex.
A large scale preparation of brush border membranes is described. Solubilized by either papain or Triton X-100, the sucrase-isomaltase complex is purified in a three-step procedure, including differential centrifugation, Sephadex G-200 and DEAE-cellulose chromatography. Detergent solubilized and protease solubilized sucrase-isomaltase differ in tendency to aggregate but not in enzymatic characteristics. The chemical composition and the molecular weight of the two enzyme complexes are almost identical. Limited digestion of the Triton-solubilized sucrase-isomaltase complex by papain produces a protein electrophoretically indistinguishable from papain-solubilized sucrase-isomaltase together with low molecular proteolytic fragments.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D005959:Glucosidases / Q000302:isolation & purification* / Q000378:metabolism; D007413:Intestinal Mucosa / Q000201:enzymology; D007421:Intestine, Small / Q000201:enzymology*; D007700:Kinetics; D008320:Maltose; D009097:Multienzyme Complexes / Q000302:isolation & purification* / Q000378:metabolism; D010206:Papain; D011092:Polyethylene Glycols; D011817:Rabbits; D012964:Sodium / Q000494:pharmacology; D012995:Solubility; D013393:Sucrase / Q000302:isolation & purification* / Q000378:metabolism
D000596:Amino Acids; D009097:Multienzyme Complexes; D011092:Polyethylene Glycols; D008320:Maltose; D012964:Sodium; D005959:Glucosidases; D013393:Sucrase; D010206:Papain