Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of 14 lysosomal enzymes in chorionic villi at gestational ages of 6-12 weeks were assayed. Arylsulphatases A and B, alpha-glucosidase and beta-glucuronidase activities increased with advancing gestational age. When compared with the activity in cultured amniotic fluid cells, arylsulphatase A, beta-galactosidase, alpha-glucosidase, heparan N-sulphatase, alpha-L-iduronidase, alpha-mannosidase, neuraminidase, and sphingomyelinase showed significant differences. All except beta-glucuronidase showed lower activity in chorionic villi than in cultured amniotic fluid cells. Prenatal diagnosis using chorionic villi was possible except for alpha-L-iduronidase. Storage at -20 degrees C up to 42 days did not significantly affect activity. The results emphasize the importance of using fresh or frozen age-matched control tissue for diagnosis.
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PMID:Variation of lysosomal enzyme activity with gestational age in chorionic villi. 207 34

The maltase (EC 3.2.1.20)/glucoamylase (EC 3.2.1.3) complex from rat small intestine brush border, which is able to split alpha (1----4) glucose-sorbitol linkage, was isolated and purified by chromatography on DEAE-Trisacryl M and Sepharose 6B. The complex was homogeneous on polyacrylamide gel electrophoresis. Kinetic parameters were studied on two substrates: maltose and maltitol (Km:1.3 mM and 30 mM, Vmax:200 nmol X min-1 and 15 nmol X min-1, respectively). Inhibition studies were performed with maltose and maltitol as substrates and isomaltitol and delta-gluconolactone as inhibitors. Crossed-inhibition reactions were also performed. The results support the existence of one single catalytic site and this fact was confirmed by physicochemical properties. Similar results were obtained with germ-free rats as well as with conventional rats adapted over 6-12 months to Lycasin 80/55 as the sole source of sugar. Lycasin 80/55, hydrogenated starch hydrolysate, was converted by purified maltase/glucoamylase complex in glucose and sorbitol.
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PMID:New approach to the metabolism of hydrogenated starch hydrolysate: hydrolysis by the maltase/glucoamylase complex of the rat intestinal mucosa. 392 78

Cultured human skin fibroblasts from control persons and from patients with the generalized and late-onset forms of Pompe's disease were labelled with radioactive leucine and the incorporation of radioactivity into acid alpha-glucosidase and cathepsin D was analysed by immunoprecipitation, gel electrophoresis and fluorography. When the labelling was carried out for 6-12 h in the presence of NH4Cl, the labelling of secreted alpha-glucosidase relative to that of secreted cathepsin D in fibroblasts from patients with the late-onset form of Pompe's disease was less than 15% of that in fibroblasts from control persons. However, when the fibroblasts were labelled for less than 1 h, the relative rate of incorporation of radioactivity into acid alpha-glucosidase was rather similar in the two types of fibroblasts. In fibroblasts from patients with the generalized form of Pompe's disease no incorporation of radioactivity into acid alpha-glucosidase could be detected.
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PMID:Biosynthesis of acid alpha-glucosidase in late-onset forms of glycogenosis type II (Pompe's disease). 676 Nov 45

Dietary flexibility in digestive enzyme activity is widespread in vertebrates, but mechanisms are poorly understood. When laboratory rats are switched to higher carbohydrate diet, activity of intestinal sucrase-isomaltase (SI) increases within 6-12 h, mainly by rapid increase in enzyme transcription followed by rapid translation and translocation to the intestine's apical, brush border membrane (BBM). We performed the first unified study of the overall process in birds, relying on activity, proteomic and transcriptomic data from nestling house sparrows (Passer domesticus). They switch naturally from low-starch insect diet to higher-starch seed diet, and SI is responsible for all their intestinal maltase and sucrase activities. Twenty-four hours after a switch to a high-starch diet, SI activity was increased, but not at 12 h post-diet switch. SI was the only hydrolase increased in the BBM, and its relative abundance and activity were positively correlated. Twenty-four hours after a reverse switch back to the lower-starch diet, SI activity was decreased, but not at 12 h post-diet switch. Parallel changes in SI mRNA were associated with the changes in SI activity in both diet switch experiments. This is the first demonstration that birds may rely on rapid increase in abundance of SI and its mRNA when adjusting to high starch diet. Although the mechanisms underlying dietary induction of intestinal enzymes seem similar in nestling house sparrows and laboratory rodents, time course for modulation in nestlings seemed half as fast compared to laboratory rodents. This may be understandable considering differences in ecology and evolution.
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PMID:Dietary adaptation to high starch involves increased relative abundance of sucrase-isomaltase and its mRNA in nestling house sparrows. 3317 89