Studies on the intestinal disaccharidases of the pigeon. II. Subcellular localization and solubilization.
In the pigeon, 70-80% of the activities of maltase (alpha-D-glucoside glucohydrolase EC 3.2.1.20), sucrase (alpha-glucohydrolase, EC 3.2.1.48), isomaltase (dextran 6-alpha-D-glucan hydrolase, EC 3.2.1.10) and glucoamylase (1,4-alpha-D-glucan glucohydrolase, EC 3.2.1.3) were found to be localized in the brush-border membrane of intestinal epithelial cells. Of the total glycosidase activities in the mucosal homogenate, nearly 60 to 70% were recovered in the microsomal (105 000 X g) fraction, about 30% in the mitochondrial (22 000 X g) fraction and less than 5% from the cytosol (105 000 X g supernatant) fraction. The hydrolases were solubilized by digestion with papain but not with trypsin, and the phosphate ion had a protective effect in the solubilization. Amongst detergents, Triton X-100 but not sodium deoxycholate, was found to truly solubilize these enzymes.
D000818:Animals; D010856:Columbidae / Q000378:metabolism*; D004186:Disaccharidases / Q000302:isolation & purification / Q000378:metabolism*; D006868:Hydrolysis; D066298:In Vitro Techniques; D007413:Intestinal Mucosa / Q000201:enzymology; D007422:Intestines / Q000201:enzymology*; D008871:Microvilli / Q000201:enzymology; D009696:Nucleic Acids / Q000378:metabolism; D011506:Proteins / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology*
D009696:Nucleic Acids; D011506:Proteins; D004186:Disaccharidases