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

The beige mouse is an animal model for the human Chediak-Higashi syndrome, a disease characterized by giant lysosomes in most cell types. In mice, treatment with androgenic hormones causes a 20-50-fold elevation in at least one kidney lysosomal enzyme, beta-glucuronidase. Beige mice treated with androgen had significantly higher kidney beta-glucuronidase, beta-galactosidase, and N-acetyl-beta-D-glucosaminidase (hexosaminidase) levels than normal mice. Other androgen-inducible enzymes and enzyme markers for the cytosol, mitochondria, and peroxisomes were not increased in kidney of beige mice. No significant lysosomal enzyme elevation was observed in five other organs of beige mice with or without androgen treatment, nor in kidneys of beige females not treated with androgen. Histochemical staining for glucuronidase together with subcellular fractionation showed that the higher glucuronidase content of beige mouse kidney is caused by a striking accumulation of giant glucuronidase-containing lysosomes in tubule cells near the corticomedullary boundary. In normal mice lysosomal enzymes are coordinately released into the lumen of the kidney tubules and appreciable amounts of lysosomal enzymes are present in the urine. Levels of urinary lysosomal enzymes are much lower in beige mice than in normal mice. It appears that lysosomes may accumulate in beige mice because of defective exocytosis resulting either from decreased intracellular motility of lysosomes or from their improper fusion with the plasma membrane. A similar defect could account for characteristics of the Chediak-Higashi syndrome.
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PMID:Defective lysosomal enzyme secretion in kidneys of Chediak-Higashi (beige) mice. 0 Apr 8

Changes of activity of several glycosidases (beta-galactosidase, beta-glucuronidase, N-acetyl-beta-D-glucosaminidase, alpha-D-mannosidase and alpha-L-fucosidase) were compared in the forebrain and cerebellum during postnatal development of the rat. Detailed analysis of the data showed similarities, but also substantial differences in their development in both organs. This is interpreted as an indication of the presence of common regulatory mechanisms, as well as of other factors which differently influence development of the glycosidases studied in both CNS parts.
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PMID:Comparison of postnatal development of several acid glycosidases in the rat forebrain and cerebellum. 2 Jan 69

Activities of acid phosphatase, beta-glucuronidase, N-acethyl-beta-D-glucosaminidase and acid beta-galactosidase were investigated histochemically in rabbit corneas. Frozen sections after block fixation in cold 4% formaldehyde with 1% CaCl2 followed by washing in cold physiological saline as well as cold microtome sections of corneas quenched in petroleter chilled with acetone-dry ice mixture, transferred to nonprecooled slides or semipermeable membranes were used. Standard aqueous media were employed in the case of free-floating frozen sections of fixed corneas as well as of cold mictrotome sections (postfixed in cold 4% formaldehyde). Agar media were used in connection with the technic of semipermeable membranes. Gomori method (in the case of acid phosphatase), simultaneous azocoupling methods (substrates derivated of naphthol-AS-BI with hexazonium-p-rosanilin) in the case of acid phosphatase, beta-glucuronidase and N-acetyl-beta-D-glucosaminidase and the indigogenic method in the case of acid beta-galactosidase were applied. Enzyme activities in sections of fixed corneas were minimal in comparison with those in cold microtome sections of unfixed material revealed particularly with the technic of semipermeable membranes which is to be preferred. This technic is recommended in studies concerned with lysosomal enzymes in the cornea, particularly in keratocytes. All enzymes investigated were present in corneal epithelium, keratocytes and endothelium. Acid phosphatase displayed the highest activity followed by beta-glucuronidase and acetyl-beta-D-glucosaminidase. The activity of beta-galactosidase was the lowest. For the demonstration of activities in keratocytes sections parallel to the surface are very suitable. In these sections enzyme activities were demonstrated in small granules (apparently lysosomes) present in the central part of their cytoplasm as well as in projections. Diffuse staining was also seen, being the highest in the case of acid phosphatase.
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PMID:Distribution of acid phosphatase, beta-glucuronidase, n-acetyl-beta-d-glucosaminidase and beta-galactosidase in cornea of albino rabbit. 5 44

Three urinary lysosomal enzymes, beta-glucuronidase (beta-Gluc), beta-galactosidase (beta-Gal) and N-acetyl-beta-D-glucosaminidase (NAG), were measured in twenty-one renal allograft recipients to evaluate their role in the diagnosis and prediction of rejection episodes, and in the prediction of eventual graft outcome. A fluorometric assay using methylumbelliferone substrates was used to measure the three enzymes in morning urine samples and enzyme activity was defined in terms of urine creatinine concentration. Urinary NAG levels increased significantly in 13/16 first rejection episodes and 4/4 instances of acute tubular necrosis and graft infarction. In 5 of the 16 first rejection episodes the NAG was predictive of the rejection. NAG was not useful in diagnosing second or subsequent rejections and beta-Gluc and beta-Gal were of little value in assessing any component of renal transplant pathology. As a prognostic index of eventual graft outcome, the peak urinary NAG was particularly encouraging. It correlated strongly with deterioration in graft function as time passed such that only 2/10 patients with peak NAG greater than 1400 Units had normal serum creatinines at 6 months post transplantation. Conversely 4/4 patients with peak NAG levels less than 700 Units had normal serum creatinine at that time. In our series the measurement of urinary NAG was a useful adjunct to the diagnosis of first rejections but appears to be more valuable in predicting graft outcome.
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PMID:Urinary lysosomal enzyme excretion after renal allotransplantation. 10 10

The activities of acid phosphatase, beta-glucuronidase, beta-galactosidase, and N-acetyl-beta-D-glucosaminidase were investigated in the normal rabbit cornea. For all spectrophotometric assays, appropriate p-nitrophenyl derivates were used. Only beta-glucuronidase were determined employing phenolphthalein glucuronid as a substrante. Acid phosphatase revealed the highest activity, followed by N-acetyl-beta-D-glucosaminidase and beta-galactosidase. In the case of beta-glucuronidase the lowest activity was found. The results on the rabbit cornea are compared with those on some other tissues described in the literature. Correlation of biochemical data and histochemical findings in the same species is briefly discussed.
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PMID:Biochemical study on some acid hydrolases in the normal rabbit cornea. 30 56

On the basis of experimental research results a method to assess the functional state of pulmonary alveolar macrophages in rabbits and rats has been proposed as a criterion of the biological effect of chemical atmospheric pollutants. The test involves a cytological assay, determination of the viable cells quantity and of the phagocytic competence, and also the biochemical study of alveolar macrophages enzymes activity (acid phosphatase, beta-glucuronidase, lysozyme, beta-galactosidase, beta-glucosidase, N-acetyl-beta-D-glucosaminidase). It has been shown that this method is informative and reliably reproducible, and that it was reasonable to use it in environmental health and other branches of experimental biology and medicine.
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PMID:[Method of studying the functional state of pulmonary alveolar macrophages during exposure to atmospheric pollutants]. 71 64

A number of adsorbents useful for purifying glycosidases were synthesized and their adsorption and characteristics were examined using partially purified glycosidase mixtures from Takadiastase or soybean. These adsorbents were prepared by coupling di-epsilon-aminocaproyl-p-aminophenyl N-acetyl-1-thio-beta-D-glucosaminide, beta-D-glucoside, beta-D-galactoside or alpha-D-mannoside with CNBr-activated Sepharose 4B. Many glycosidases were adsorbed on the four adsorbents at low ionic strength, and increase of the ionic strength caused the enzymes to be eluted. However, the specificity of the adsorbents, contrary to our expection, was very low. All of these adsorbents adsorbed Taka N-acetyl-beta-D-glucosaminidase [EC 3.2.1.30], Taka beta-D-glucosidase [EC 3.2.1.21], and Taka beta-D-galactosidase [EC 3.2.1.23] at low ionic strength. The order of elution of these three enzymes by a linear gradient of ionic strength was the same in the four adsorbents, the order being beta-D-galactosidase, beta-D-glucosidase, and N-acetyl-beta-D-glucosaminidase. Soybean glycosidases also showed nearly the same elution pattern, though the ionic strength of the eluate was slightly lower than with Taka glycosidases. Soybean alpha-D-mannosidase [EC 3.2.1.24] was also adsorbed on these adsorbents, and was eluted between beta-D-glucosidase and N-acetyl-beta-D-glucosaminidase. These adsorption phenomena were not specific as regards the structure of the glycoside moiety, but they were useful for purifying glycosidases, possessing good reproducibility with easy activation and mild operating conditions.
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PMID:Affinity chromatography of glycosidases. Preparation and properties of affinity column adsorbents. 94 2

In alkali burned rabbit corneas activities of beta-glucuronidase, N-acetyl-beta-D-glucosaminidase and acid beta-galactosidase were studied histochemically in various time intervals after the traumatization. The technic with semipermeable membranes was employed. Within four days after the injury enzyme activities in the traumatized area were almost lacking. The corresponding activities in the unaffected part of the cornea were within the norm. On the 7th day enzyme activities were on an increase (but still subnormal) in the traumatized area. This area was surrounded by a zone of keratocytes with high levels of enzyme activities. This was particularly remarkable in keratocytes subjacent to the epithelium. The activation of all enzymes studied was present in the basal layer of the epithelium and in the endothelium as well. On the 14th day enzyme activities in the traumatized area were nearly restored and on the 32nd day they could not be distinguished from the normal cornea. Beta-galactosidase displayed a relatively maximal increase in the activity of all enzymes investigated.
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PMID:Alkali burns of the rabbit cornea. I. A histochemical study of beta-glucuronidase, beta-galactosidase and N-acetyl-beta-D-glucosaminidase. 119 85

The mannitol influence on mutagenesis of ionizing radiation and cyclophosphate has been studied in albino mongrel rats using the methods of genetic and biochemical analysis. N correlation is determined between antimutagenic action of this preparation and a decrease of malondialdehyde content in cells and free fractions of matrix lysosomes (beta-galactosidase; N-acetyl-beta-D-glucosaminidase) and firmly membrane-structurized microsomal (glucose-6-phosphatase) enzymes, whose level increases under the influence of mutagens. It is shown that, one of the way of antimutagenic actions of mannitol is connected with mutagenesis correction at the stage of origin of mutagenic products and their transport to chromosome DNA.
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PMID:[The interrelation of the antimutagenic action of mannitol to its effect on cellular metabolic processes]. 129 65

The serum concentrations of FSH, LH, prolactin, testosterone, and estradiol and the enzymatic activities of hyaluronidase, glucosidases (alpha-glucosidase, beta-glucosidase, alpha-mannosidase, N-acetyl-beta-D-glucosaminidase, beta-glucuronidase, and beta-galactosidase), lactate dehydrogenase and its isoenzymes (LDH1, LDH2, LDH3, LDH-X, LDH4), and total proteins were measured in the semen of 69 subjects (8 normozoospermic controls, 7 secretory, and 54 excretory azoospermic subjects). FSH levels rose with the deterioration in spermatogenesis and served to differentiate the secretory from the excretory azoospermias. The only source of hyaluronidase and LDH-X in the ejaculate is the spermatozoa. alpha-Glucosidase activity essentially originates in the epididymis. The seminal determination of alpha-glucosidase and, to a lesser extent, alpha-mannosidase and N-acetyl-beta-D-glucosaminidase helps rapidly, sensitivity, reliably, and noninvasively to differentiate secretory azoospermias (with higher enzymatic activity) from the excretory type (less enzymatic activity) and may be of use in identifying with a certain degree of reliability the site of obstruction in the male genital tract.
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PMID:Enzyme and hormonal markers in the differential diagnosis of human azoospermia. 153 Mar 67


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