Occurrence and properties of fetal intestinal glycosidases (disaccharidases) in human amniotic fluid.
alpha-Glucosidase, beta-glucosidase and beta-galactosidase were studied in cell-free amniotic fluid samples using corresponding 4-methylumbelliferyl-glycosides and a series of disaccharides (maltose, sucrose, trehalose, turanose, cellobiose, gentiobiose and lactose) as substrates. The glycosidases exhibited several properties of intestinal disaccharidases such as pH optimum between 5.2 and 6.4, more activity towards the disaccharides than the artificial substrates, tight association of the activities with sedimentable complexes and beta-glucosidase and beta-galactosidase activities exerted by a single catalytic site. With the disaccharides as substrates, the amniotic fluid glycosidase activities were well correlated to those reported in the literature for fetal intestine of corresponding gestational ages. The presence of intestinal disaccharidases in amniotic fluid indicates that the fetal intestine contributes to the protein and enzymes of amniotic fluid.
D000653:Amniotic Fluid / Q000201:enzymology*; D002474:Cell-Free System; D004187:Disaccharides / Q000378:metabolism; D005260:Female; D005333:Fetus / Q000201:enzymology*; D005696:Galactosidases / Q000032:analysis; D005865:Gestational Age; D006026:Glycoside Hydrolases / Q000032:analysis; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007422:Intestines / Q000201:enzymology*; D009005:Monosaccharides / Q000378:metabolism; D011247:Pregnancy
D004187:Disaccharides; D009005:Monosaccharides; D005696:Galactosidases; D006026:Glycoside Hydrolases