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)

Leukocytes were obtained from 14 healthy subjects, one patient with the infantile form, two patients with the adult variant of acid maltase deficiency, two patients with chronic myelocytic leukemia, two patients with acute myeloid leukemia, and two patients with chronic lymphotic leukemia. In addition, lymphocytes were prepared from three normal subjects, and five established lymphoid lines were used. Cells were extracted either with Triton 0, 2%, or with water followed by 0.2% Triton. alpha-Glucosidase activity was measured in water homogenates, water extracts after centrifugation, and Triton extracts, with or without antisera directed against acid maltase (EC 3.2.1.3) and renal maltase (EC 3.2.1.20). The percentage of acid and renal maltases was then calculated in each soluble fraction. Normal whole leukocytes (mostly granulocytes) contain both acid and "renal" maltases, whereas normal lymphocytes contain very little or no "renal maltase." This isozyme is present in chronic myelocytic leukemia, but is absent in acute myeloid and chronic lymphocytic leukemia as well as in established lymphoid lines. Acid maltase is almost completely extracted with water, whereas renal maltase is extracted only with Triton. From the results, it appears that for the diagnosis of alpha glucosidase deficiency, cells should be extracted in water and centrifuged before determination. Lymphocytes, which are devoid of renal maltase, are a better diagnostic material than are granulocytes.
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PMID:White blood cells and the diagnosis of alpha-glucosidase deficiency. 676 91

Maltase/glucoamylase from the rat intestinal brush-border membrane was solubilized by homogenization of the intestinal mucosa in buffer containing 0.5% Triton X-100. After removal of the detergent with butan-1-ol, the enzyme was purified by chromatography on Sepharose 4B and DEAE-cellulose. The final specific activity was 70.3 units/mg of protein in six preparations, comparing favourably with the specific activity of 65.0 units/mg of protein of a pure papain-solubilized maltase/glucoamylase previously isolated and characterized by us [Flanagan & Forstner (1978) Biochem. J.173, 553-563]. The two enzymes were compared. Both migrated as single bands with the same mobility on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, were eluted at the same volume from Sepharose 4B, and had the same sedimentation pattern in mannitol gradients. The amino acid composition was similar; content of total apolar residues differed by 1.0mol%. Antibodies prepared against either enzyme gave identical precipitin lines with each. Neither enzyme bound tritiated Triton X-100. The only difference noted was the tendency of the detergent-solubilized enzyme to aggregate on storage, whereas the papain-solubilized enzyme remained unchanged. Both enzymes had two N-termini, glycine and arginine. When the two enzymes were dissociated by boiling in sodium dodecyl sulphate, each exhibited the same five species on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. Single N-termini were found in the two smaller species, 1 (glycine) and 2 (arginine), whereas larger species (3-5) had both N-terminal amino acids. Both the Triton- and papain-solubilized enzymes appear to be oligomers of species 1 and 2, indicating that the native enzyme contains two subunit types. Aggregation in aqueous solutions does not depend on a proteolytically susceptible peptide fragment at the N-terminus of either subunit.
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PMID:Isolation of a detergent-solubilized maltase/glucoamylase from rat intestine and its comparison with a maltase/glucoamylase solubilized by papain. 677 61

Lactase, maltase and sucrase activities were determined in samples of jejunal mucosa obtained by suction biopsy from 60 healthy adult German males. Primary adult hypolactasia ("lactase deficiency") was found in 8 subjects (13%). Maltase:lactase and sucrase:lactase activity ratios were significantly higher in post-weaning hypolactasia than in adult lactase persistence. Sources of variation in disaccharidase activities measured in biopsy tissue homogenates are discussed.
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PMID:Intestinal disaccharidase activities and activity ratios in a group of 60 adult German subjects. 678 Apr 38

The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated. Lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, alpha-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partum and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased. The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4.6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid beta-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid alpha-glucosidase early in lactation and of a brush border neutral maltase in adult animals. The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young.
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PMID:Intestinal lactase (beta-galactosidase) and other glycosidase activities in suckling and adult tammar wallabies (Macropus eugenii). 678 21

The activities of maltase, lactase, alkaline phosphatase and enterokinase were followed in the small intestine of rats during prenatal development. These enzymes were detectable only after the 17th day of gestation. Furthermore, each enzyme exhibited a different pattern of prenatal presence. Maltase activity appeared first (day 18), followed by lactase and alkaline phosphatase (day 19) and then enterokinase (day 20). Except for enterokinase, all of the enzymes attained a level of activity close to the newborn levels at the final day of gestation. Induced intrauterine growth retardation during the 3rd trimester led to a decrease in intestinal weight proportional to the reduction of body weight. These decrease in size of the small intestine was caused by a reduction in cell number rather than cell size. Induced intrauterine growth retardation also resulted in a selective reduction in the specific activities of lactase and alkaline phosphatase, but not of enterokinase and maltase. These results suggest that reduction in maternofetal blood flow in the 3rd trimester of gestation will cause a selective decrease in some brush border enzymes (lactase and alkaline phosphatase) but does not effect others (maltase and enterokinase).
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PMID:Effect of intrauterine growth retardation on the activities of fetal intestinal enzymes in rats. 678 32

Jejunal sucrase is known to display glucocorticoid responsiveness from birth through day 17 but not beyond that age. The aim of the current study was to determine whether this abrupt loss of responsiveness was shared by maltase, lactase, and acid beta-galactosidase. Glucocorticoid concentrations were manipulated by both adrenalectomy (ADX) and by administration of cortisone acetate (CA). Surgery or treatment was performed on each day from 16--22 days of age. Maltase activity was reduced by ADX at day 18 and earlier and was increased by CA at days 16 and 17. There were no effects at later ages. Acid beta-galactosidase was increased by ADX only at day 18 and earlier and was decreased by CA only at day 16. Lactase activity was increased by ADX at all ages up to and including day 20 but was reduced by CA only at days 16 and 17. Thus, we conclude that loss of glucocorticoid responsiveness at a relatively early stage of development is a common feature of both brush-border and lysosomal enzymes of the small intestine.
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PMID:Coordinate loss of glucocorticoid responsiveness by intestinal enzymes during postnatal development. 680 95

Female rats of the Wistar strain, weighing 40-60 g were used to study the effect of fish meals (Coryphaenoides rupestris, Chimaera monstruosa and Merluccius merluccius) on the disaccharidases and alkaline phosphatase in the small intestine in relation to the control group which consumed casein. Fish meal diets diminished lactase and alkaline phosphatase activity, the latter being most remarkable in animals fed Ch. monstruosa meal, while no statistical variations in maltase and sucrase activity were observed. Maltase, sucrase and lactase activity of animals fed Ch. monstruosa meal dropped in comparison with those fed C. rupestris meal, while the alkaline phosphatase activity showed no significant changes.
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PMID:[Effect of various fish meals on disaccharidases and alkaline phosphatase of the small intestine in rats]. 681 26

Maltase from Saccharomyces cerevisiae-II was purified by ion-exchange chromatography on DEAE-Sephadex A-50 and isoelectric focusing. The purification procedure resulted in two enzyme isoforms with pI of 5.35 and 5.3 and identical specific activities. The molecular weights of the isoforms as determined by SDS polyacrylamide gel electrophoresis and gel filtration through Sephadex G-100 are 60 000 and 55 000, respectively. Both isoforms were electrophoretically polydisperse. The maltase isoforms are glycoproteins containing 1.5-2% of glucosamine and 5-8% (isoform A) and 2-3% (isoform B) of neutral sugars. Using paper chromatography and glucose oxidase, it was shown that glucose is an indispensable constituent of neutral sugars in both isoforms.
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PMID:[Isolation and properties of maltase from Saccharomyces cerevisiae-II]. 701 1

The effect of four raw legume diets: field beans (Vicia faba) (RFB), navy beans (Phaseolus vulgaris) (RNB), soybeans (Glycine soja) (RSB) and bitter vetch (VICIA ervilia) (RBV), on disaccharidase activities in chick small intestine have been studied. Maltase and sucrase activities, which vary with age, were determined in 1 to 60 day old animals, RFB and RBV diets had no effect on maltase activity and only increased sucrase activity in 60 day old chicks. Both maltase and sucrase activities decreased in chicks on RSB diet, regardless of their age, and the decrease was even more pronounced in chicks on RNB diet. Contrarywise, chicks fed on autoclaved navy beans and soybeans showed a considerably higher activity of these disaccharidases.
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PMID:Effect of raw legume diets on disaccharidase activity in the small intestine of chicks. 719 9

In two groups of 16 animals each lambs were fed restrictively resp. ad libitum withour ewes with a milk replacer up to the age of four weeks. Maltase activity in the contents of the duodenum and the pancreas homogenate increased with the increasing age of the lambs. The maltase activity of the restrictively fed lambs was higher. The maltase activity in the duodenal mucosa was not influenced by the age. Lactase activity in the duodenal mucosa showed a decreasing tendency up to the end of the four week of life; an increase of lactase activity in the contents of the duodenum could be ascertained up to the fourth week. In comparison with the suckling lambs reared by ewes (cf. 1.) the maltase activity in the duodenal mucosa of the lambs reared without ewes was lower and that in the contents of the duodenum was higher. Concerning lactase activity, there were not significant differences between the rearing and feeding regimens up to the age of three weeks. At the end of their fourth week of life the lactase activity in the suckling lambs was significantly lower than that in the lambs reared without ewes. The total maltase activity (= sum of the activities in the duodenal mucosa, the contents of the duodenum and in the pancreas) showed the highest values for the lambs reared without ewes and fed restrictively in the first three weeks of life. Saccharase activities in the duodenal mucosa or the contents of the duodenum could not be detected in any case.
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PMID:[Studies of the activity of disaccharides in growing sheep. 2. The influence of the feeding regime on the activity of disaccharidases in lambs up to the age of 4 weeks under various rearing conditions]. 728 31


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