Sucrase-isomaltase: a stalked intrinsic protein of the brush border membrane.
The isolation and purification of sucrase-isomaltase from brush border membrane is described and the physicochemical properties of the pure enzyme are discussed. Our present understanding of the mode of association of the intrinsic membrane protein sucrase-isomaltase with the brush border membrane will be the central point of this contribution. The assembly of sucrase-isomaltase into phospholipid bilayers has been reported to result in a model membrane system which resembles the "native" brush border membrane as regards the mode of lipid-protein interaction. The physicochemical properties of this reconstituted model membrane will be compared to the in vivo situation as represented by brush border membrane vesicles routinely isolated from small intestinal brush borders. The biosynthetic mechanism will be discussed.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D002627:Chemistry, Physical; D003902:Detergents; D008055:Lipids; D008871:Microvilli / Q000201:enzymology*; D009097:Multienzyme Complexes / Q000378:metabolism*; D010447:Peptide Hydrolases; D011487:Protein Conformation; D013394:Sucrase-Isomaltase Complex / Q000302:isolation & purification / Q000378:metabolism*
D000596:Amino Acids; D003902:Detergents; D008055:Lipids; D009097:Multienzyme Complexes; D013394:Sucrase-Isomaltase Complex; D010447:Peptide Hydrolases