Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.23 (beta-galactosidase)
 14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of N-acetyl-beta, D-glucosaminidase (NAG, EC 3.2.1.30), beta, D-galactosidase (beta-gal, EC 3.2.1.23) and acid phosphatase (ac-Pase, EC 3.1.3.2) were measured in the glomeruli, five segments of the proximal and four segments of the distal tubule of normal male Wistar rats. The activities of NAG and beta-gal are 3- to 5-fold higher in the first part of the proximal tubule than in other segments and very low in glomeruli. We propose that the distribution of these two glycosidases reflects the contribution of the different tubular segments to the reabsorption of glycoproteins. The maximal activity of ac-Pase was found in the straight part of the proximal tubule. It was only 1.5-fold higher than in the distal tubule. Moreover, the activity in glomeruli is rather high. We conclude that ac-Pase is not primarily involved in the handling of reabsorbed molecules.
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PMID:Quantitative distribution of lysosomal hydrolases in the rat nephron. 50 Apr 8

1. Comparative studies of beta-N-acetylglucosaminidase (NAG, EC 3.2.1. 52) and beta-galactosidase (EC 3.2.1. 23) activities, protein concentration and creatinine clearance, were carried out in urine and kidney from guinea pigs treated with "toxic oil", orally administered under different conditions, related to controls. 2. Enzyme activities did not vary significantly in urine with any of the studied conditions of oil administration. By contrast, in kidney, beta-D-galactosidase disclosed a significant increase in all the treatments studied when compared to controls without treatment. 3. Urinary protein excretion, creatinine concentration and creatinine clearance were significantly greater in treated animals than in controls after 4 weeks of treatment. 4. Relative kidney weight (g/100 g body wt), was significantly lower in animals treated for 28 days with previously heated oil.
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PMID:Toxic oil syndrome: a study of renal function in guinea pigs fed toxic oil. 810 39

beta-N-Acetylglucosaminidase and beta-galactosidase activities were determined in serum and liver from guinea pigs fed "toxic oil" (related to cases of TOS) under different experimental conditions. The results obtained were compared with those of guinea pigs fed non "toxic oil" (case-unrelated oil; controls 1) and animals fed no oil (controls 2). In serum, both activities were significantly increased after all treatments with case-related oil as compared with controls 1 and 2. In the liver, beta-galactosidase activity did not show significant differences in any of the treatments when compared with controls 2. However, NAG activity decreased significantly after 7 days of treatment with non-heated oil--either case-related or not--when compared with controls 2; it also decreased significantly after 28 days of treatment with heated case-unrelated oil, both with respect to controls 2 and the animals fed case-related oil. Liver weights tended to increase in the animals fed oil--toxic or not--with respect to those of the livers from untreated animals. Morphologically, a slight vacuolization of the hepatocytes was observed in some of the samples from the treated animals.
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PMID:Lysosomal enzyme activities in liver and sera from guinea pigs fed oil related to the toxic oil syndrome. 824 Jul 21

Ursodeoxycholic acid 7-N-acetylglucosaminides (UDCA 7-NAGs) are novel conjugated metabolites whose urine levels are expected to be a specific diagnostic index for primary biliary cirrhosis. To obtain a specific antibody which is useful for developing immunochemical analytical methods of UDCA 7-NAGs, a variety of monoclonal antibodies have been generated. Spleen cells from an A/J mouse, which had been immunized with a conjugate of nonamidated UDCA 7-NAG and bovine serum albumin, were fused with P3/NS1/1-Ag4-1 myeloma cells. After screening by an enzyme-linked immunosorbent assay (ELISA) using a beta-galactosidase-labeled antigen, thirteen kinds of antibody-secreting hybridoma clones were established. Binding properties of these monoclonal antibodies were investigated in detail by ELISA. One of these antibodies, Ab-#8 (gamma1, kappa) had the most favorable characteristics for clinical application, which was group-specific to the 7-NAG conjugates of nonamidated, glycine- and taurine-amidated UDCAs providing a highly sensitive dose-response curve for each conjugate (midpoint 17 pg per assay for nonamidated UDCA 7-NAG). Cross-reactivities with eleven kinds of bile acids, including some potential interfering metabolites as UDCA 3-sulfate, were negligibly low. By using direct ELISA based on Ab-#8, daily urinary excretion rates of UDCA 7-NAGs of two healthy subjects were determined to be 1030 and 469 microg as GUDCA 7-NAG equivalent.
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PMID:Production and characterization of group-specific monoclonal antibodies recognizing nonamidated, glycine- and taurine-amidated ursodeoxycholic acid 7-N-acetylglucosaminides. 960 11

The present study describes the activity and localisation of three putative lysosomal marker enzymes, acid phosphatase (AP), N-acetyl-beta-D-glucosaminidase (beta-NAG), and beta-galactosidase (beta-Gal), in whole individuals and in distinct parts of the earthworms, Eisenia veneta and Eisenia fetida. Activities of AP and beta-NAG were high in the two species with most of the activity located to the anterior and mid-parts of the worms. The activity of beta-Gal was low in all body regions. We found interspecies difference in the AP activity as E. veneta had significantly higher activity of AP than E. fetida in posterior and mid-parts, as well as in whole individuals. Of the three enzymes tested, AP was the only enzyme located to lysosomes, yielding high latency all over the worms with especially high latency in the coelomic fluids and posterior regions. The lysosomal APs in E. veneta and E. fetida may be utilised as a new biomarker for xenobiotic-induced lysosomal membrane damage in earthworms.
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PMID:Activity and localisation of the lysosomal marker enzymes acid phosphatase, N-acetyl-beta-D-glucosaminidase, and beta-galactosidase in the earthworms Eisenia fetida and E. veneta. 1081 77

The mammalian epididymis is an organ particularly rich in acid hydrolases, consistent with a developed lysosomal apparatus. However, some of these enzymes could also play a role in an extracellular environment, since they are actively secreted by the epithelium. In this study the authors measured the activity of five acid hydrolases distributed between the epithelium, fluid, small vesicles, and spermatozoa of the rat cauda epididymis in adult rats, and compared with that distribution under conditions of deprivation of luminal testosterone and testicular compounds (hemicastration). Lysosomal enzymes are differently compartmentalized in rat cauda epididymis. Most of beta-galactosidase (beta-GAL) and aryl sulfatase (approximately 70%) were found in soluble form within the fluid. Some 60% of N-acetyl-beta-D-glucosaminidase (beta-NAG) and alpha-mannosidase (alpha-MAN) become transiently bound to sperm, and beta-glucuronidase (beta-GLU) was mostly concentrated in the epithelium. After remotion of testis this distribution changed, as the retention of alpha-MAN, beta-GAL, beta-GLU, and beta-NAG by the epididiymal tissue increased. The increase of beta-GLU followed an increase of synthesis of the enzyme. The distribution of enzymes in the epididymis from the contralateral side was similar to that in normal rats. The different roles for each enzyme in the epididymis are discussed.
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PMID:Compartmentalization of lysosomal enzymes in cauda epididymis of normal and castrated rats. 1196 12