Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

gamma-Glutamyl transpeptidase (gamma-GT), an enzyme possibly involved in amino acid transport, was investigated in rat small intestine using the synthetic substrate L-gamma-glutamyl-p-nitroanilide. Enzyme localization and characteristics were correlated with features of amino acid uptake. gamma-GT activity copurified with sucrase and alkaline phosphatase. Activity was maximal at pH 8.2 and was stimulated by monovalent cations. The relative specificity of the gamma-GT reaction with diglycine and eight essential amino acids as substrates correlated well with the rate of intestinal absorption of this dipeptide and these amino acids as observed by others. gamma-GT activity was 12-fold greater in the jejunum than in the ileum, again in agreement with relative rates of amino acid absorption along the length of rat intestine. The specific activity of gamma-GT in villus tip cells was 10 times greater than in crypt cells, and amino acid uptake was 2 to 6 times greater with villus tip than with crypt cells. Bromosulfophthalein, a noncompetitive inhibitor of gamma-GT, inhibited amino acid uptake. These studies support the concept that membrane gamma-GT may be involved in amino acid and dipeptide uptake, and indicate that further investigation of such involvement may be conveniently pursued using mammalian small bowel.
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PMID:gamma-glutamyl transpeptidase of rat intestine: localization and possible role in amino acid transport. 0 32

Brush borders free of nuclei were isolated by repeated homogenization and centrifugation in iso-osmotic medium. They showed typical morphology under electron microscopy. The mean recovery and enrichment of alkaline phosphatase activity in the brush-border fraction were 50% and 17.5-fold respectively. gamma-Glutamyl transpeptidase showed a close parallelism with alkaline phosphatase and sucrase in subcellular distribution. Microvillar membranes were purified from isolated brush borders; they showed a further enrichment for alkaline phosphatase and were composed of homogeneous vesicles. Both brush-border and microvillar-membrane preparations were analysed for contamination by basolateral and endoplasmic-reticular membranes. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of the microvillar-membrane preparation in six different systems revealed approx. 40 components in the mol.wt. range 15 000-232 000. They were grouped into seven major classes on the basis of molecular weight and electrophoretic patterns.
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PMID:Characterization of brush borders purified in iso-osmotic medium and microvillar membranes subfractionated from mouse small intestine. 731 8