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

The effect of a new complex oligosaccharide (Bay g 5421) of microbial origin on human intestinal alpha-glucosidehydrolase activity was tested in mucosal homogenate from human small bowel biopsy specimens. The alpha-glucosidehydrolase inhibitor (alpha-GHI) exerted a potent inhibitory effect on glucoamylase, sucrase, and maltase, was minimally effective on isomaltase, and did not affect trehalase and lactase activity. Kinetic analysis revealed a fully competitive type of inhibition with a Ki of 1.3 x 10(-6) M; thus the inhibitor had a 15,000-fold higher affinity to the enzyme sucrase than its natural substrate sucrose. The new compound may prove to be useful in the study of carbohydrate maldigestion and malabsorption and may possibly be of therapeutic benefit in diabetes and obesity.
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PMID:Inhibition of human intestinal alpha-glucosidehydrolases by a new complex oligosaccharide. 44 22

Using accumulating preparations of the mucose, studies have been made on the rate of accumulation of the glucose from 11 mM solutions of glucose, maltose and starch in proximal, intermediate and distal parts of the small intestine of 2--13-week rats. It was demonstrated that in 2-week animals, rather intensive transmembrane transport of "free" glucose takes place in the proximal and medial parts of the small intestine, the transport of glucose in the form of maltose or starch being absent. At later stages of postnatal life, especially to the onset of definitive nutrition, together with the induction of alpha-glucosidase systems, gamma-amylase and maltase transporting mechanisms are formed which provide for the adaptation of the organism to qualitatively new feeding conditions.
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PMID:[Postnatal formation of the mechanisms of carbohydrate hydrolysis and transport in the rat small intestine]. 51 43

Adult and suckling (13 days old) rat intestinal brush borders have been purified by the procedure of Schmitz et al. (25). Enzymatic proteins have been separated by polyacrylamide gel electrophoresis. In the adult rat, enzyme proteins have been separated by polyacrylamide gel electrophoresis. In the adult rat, enzyme activities in order from the origin were: maltase/glucoamylase/sucrase-isomaltase (protein band 3), lactase (protein band 5), maltase/sucrase-isomaltase (protein band 6) and alkaline phosphatase (protein bands 8 and 9). In the suckling rat, protein band 5 associated with lactase activity was found to be markedly higher compared to the adult rat. Gels were completely devoid of sucrase-isomaltase activity while protein band 3 was strikingly reduced and protein band 6 absent. After hydrocortisone administration to suckling rats, a new band associated with sucrase-isomaltase activity appeared in position 6, whereas protein band 3 markedly increased with the simultaneous appearance of sucrase-isomaltase activity.
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PMID:Separation and characterization of intestinal brush border enzymes in adult rats and in suckling rats under normal conditions and after hydrocortisone injections. 63 79

Brush-border membranes were isolated from the rat small intestine and then treated with sodium dodecyl sulphate under non-reducing conditions at room temperature. Analysis of the solubilized components by polyacrylamide-gel electrophoresis identified three major glycoproteins that co-migrate with glucoamylase-maltase-sucrase, lactase and isomaltase-maltase-sucrase activities. High activities of alkaline phosphatase and trehalase were detectable, but they could not be attributed to distinct co-migrating protein bands. Analysis of mucosa from the distal small intestine by the same methods showed a pattern of bands different from that obtained with the proximal intestine, which appeared to correlate with the relative deficiency of some of the enzymes in the distal region.
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PMID:The identification of rat intestinal membrane enzymes after electrophoresis on polyacrylamide gels containing sodium dodecyl sulphate. 69 63

The separation by polyacrylamide gel electrophoresis and subsequent enzymatic analysis of the components of the guinea pig intestinal brush border membrane revealed the presence of three enzyme complexes: maltase-glucoamylase, maltase-sucrase-glucoamylase and maltase-sucrase. Additional bands possessing lactase, trehalase and alkaline phosphatase activity were identified but no phlorizin hydrolase or palatinase was detectable. After exposure to strong dissociating conditions the bands possessing enzymatic activity were either absent or greatly reduced in intensity.
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PMID:Glycosidases of the guinea pig brush border membrane. 86 Dec 25

Activities of gamma-amylase (acidic alpha-glucosidase) and phosphorylase were studied in brain of normal rabbits and in animals subjected to craniocerebral trauma. The gamma-amylase activity was slightly increased within 10 min after the trauma and its was decreased within 24 hrs. The phosphorylase activity was decreased in the both periods of investigation. Administration of strychnine into normal animals increased the gamma-amylase activity and decreased the phosphorylase activity. At the same time, the normalization of the gamma-amylase activity was observed after stimulation of the central nervous system (by phenamine) of traumatized animals. Inhibition of the central nervous system of traumatized animals (by administration of urethane and barbital mixture) led to the subsequent decrease of the gamma-amylase activity (in several cases up to the zero value) without any alterations in the phosphorylase activity. Participation of gamma-amylase in glycogen metabolism of rabbit brain is discussed.
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PMID:[Glycogen degradation in rabbit brain under normal conditions and following cranio-cerebral injury]. 88 61

Intestinal mucosa and pancreas from purebred Beagle dogs were assayed for carbohydrase activity, using several methods of tissue treatment. The enzymes found and studied were alpha-amylase, sucrase, lactase, amyloglucosidase, cellobiase, maltase, and isomaltase. Experiments using polyacrylamide gel columns and heat inactivation showed the presence of an isozyme of maltase which degrades isomaltose. This activity had not been previously demonstrated in dogs. An optimal standard procedure is presented for the preparation and assay of canine digestive enzymes. A statistical analysis of variance of the results showed that the variance was primarily associated with differences among dogs and not by variance within the procedure. When the different extraction procedures were used, results indicated that the level of enzymes detected differed with the method of treatment.
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PMID:Detection and definition of canine intestinal carbohydrases, using a standardized method. 88 14

A method is described for the purification of human enterokinase from accumulated duodenal fluid by affinity chromatography using p-aminobenzamidine as the ligand. Resolution was greatest when glycylglycine was substituted as the spacer arm. Purification was not a one-step procedure, and some contamination, principally by the alpha-glucosidases, remained. Their removal was completed by immunoadsorption using antisera raised to enterokinase-free material containing these enzymes, prepared as a by-product of the purification procedure. The final preparation had an activity of 4260 nmol of trypsin/min per mg and was free of other enzymic activity tested. Amino acid and sugar analyses of the highly purified enzyme indicated an acidic glycoprotein containing 57% sugar (neutral sugars 47%, amino sugars 10%). The apparent mol.wts. and Stokes radii of human and pig enterokinase were 296 000 and 316 000, and 5.65 and 5.78 nm respectively. Two isoenzymes were identified for human enterokinase and three for the pig enzyme. Human enterokinase demonstrated a resistance to reduction of disulphide linkages and to sodium dodecyl sulphate binding, which may be related to the need for it to retain its integrity in the digestive environment of the upper small intestine. Antisera to highly purified pig and human enterokinases specifically inhibited enterokinase activity. Immuno-inhibition of intestinal aminopeptidase, maltase and glucoamylase by homologous antisera was not observed.
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PMID:The purification of human enterokinase by affinity chromatography and immunoadsorption. Some observations on its molecular characteristics and comparisons with the pig enzyme. 94 36

Acid alpha-glucosidase from human liver was 720-fold purified by means of a specific sorption on Sephadex G-150 and a specific desorption from Sephadex by the competitive inhibitor, methyl-alpha-D-glucopyranoside. The preparation obtained was homogenous in ultracentrifuge and polyacrilamide gel electrophoresis. The enzyme possessed both maltase and glucoamylase activities and splitted maltose, amylopectin and glycogen with Km values of 7mM, 7.7 mg/ml and 5 mg/ml respectively. Methyl-alpha-D-glucopyranoside competitively inhibited the enzymatic hydrolysis of polysaccharides (Ki=6.95 mM) and did not affect the maltose degradation. The sedimentation coefficient of the purified enzyme preparation was 5.4 S; in 5 M guanidine. HCl the coefficient decreased to 2.2 S, which testified to the fact that the enzyme molecule consisted of subunits.
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PMID:[Purification and properties of acid alpha-glucosidase (gamma-amylase) from the human liver]. 121 51

Two-hour heat exposure (40-41 degrees C) was shown to change the circadian rhythms of enteral gamma-amylase, maltase and sucrase activities. The character and obviousness of the changes depended on the type of enzyme activity and the portion of the small intestine. The heat exposure did not change daily mean levels of enzymatic activities and their distribution along the small intestine.
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PMID:[The effect of heat exposure on the circadian rhythm of the enzymatic activity in different sections of the rat small intestine]. 133 33


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