
pmid: 3027683
AbstractThe intestinal microvilli of fetal origin in human amniotic fluid were purified by Ca2+ precipitation of contaminating organelles followed by differential centrifugation of microvillar membranes. In the purified preparation, the specific activity of the microvillar marker‐enzymes maltase and sucrase increased about 77‐fold over that in cell‐free amniotic fluid. Significant contamination of the purified preparation by endoplasmic reticulum (microsomes) and lysosomes was ruled out on the basis of a low content of the marker enzymes glucose‐6‐phosphatase (microsomes) and acid phosphatase (lysosomes). Amniotic fluid microvilli contain typical enzymes of the fetal intestine including maltase, sucrase, trehalase, alkaline phosphatase and γ‐glutamyltransferase, and their morphology by electron microscopy resembles that of vesiculated intestinal microvilli. Prenatal detection of genetic diseases due to a deficiency of a protein expressed in these membranes or associated to abnormal microvilli seems feasible.
Microvilli, Acid Phosphatase, Alkaline Phosphatase, Amniotic Fluid, Cell Fractionation, Disaccharidases, Microscopy, Electron, Pregnancy, Glucose-6-Phosphatase, Humans, Female, Intestinal Mucosa
Microvilli, Acid Phosphatase, Alkaline Phosphatase, Amniotic Fluid, Cell Fractionation, Disaccharidases, Microscopy, Electron, Pregnancy, Glucose-6-Phosphatase, Humans, Female, Intestinal Mucosa
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