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)

Seven acid glycosidases activities have been measured in normal rat uterus during the oestrus cycle. It has been observed that alpha-fucosidase, alpha-mannosidase, beta-galactosidase, alpha-galactosidase, aryl sulfatase, acid phosphatase and hexosaminidase activities changed cyclically during the oestrus cycle. From onward oestrus to metaoestrus the enzyme activities are in their highest level, but then decline slightly towards the resting one, as the cycle progresses. It is possible that changes in glycosidases content bear a lysosomal relationship, since it is known the increase in the lysosome content of the uterus during the oestrus and metaoestrus. The increased enzyme content could be related to uterus glycoproteins secretion and degradation during the normal oestrus cycle.
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PMID:Glycosidases in the rat uterus during the oestrus cycle. 609 86

Six glycosidase activities were detected in homogenates of the rat uterus by using the p-Nitrophenyl-glycoside as substrate. The enzyme activities were separated by Sephadex G-200 column chromatography. The uterus contained alpha-galactosidase, beta-galactosidase and N-acetylglucosaminidase activity which had a similar pH optima of 4.4, whereas the pH optimum for beta-fucosidase was found to be of 4.4 - 4.6. The alpha-mannosidase activity showed two peaks of maximal activity at pH 5.0 and pH 6.0. The uterus contained two forms of the alpha-L-fucosidase activity separable by Sephadex G-200 which had a pH optima of 4.4 - 4.6 (form I) and pH 5.0 (form II). The glycosidases differed in heat stability, Km values and other several characteristics, which suggests that each enzyme apparently did not show any cross-contamination.
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PMID:Glycosidases from the rat uterus. 609 87

The chemical nature of one determinant (CFA 10) of a chicken onco-developmental antigen system was investigated using both chemical modification of cell surfaces and hapten inhibition. The presence of CFA 10 on pigeon RBC's is restricted both by the developmental status of the bird and by genetic segregation within the species. The involvement of a galactose-like structure with this determinant was suggested by the ability of alpha-galactosidase, sodium-m-periodate, and galactose oxidase to destroy CFA-10 activity. Other glycosidases including beta-galactosidase and proteolytic digestion failed to alter the antigenic determinant. Sugar inhibition assays using monospecific antisera against CFA 10 verified both the galactose-like specificity of the determinant and the possible significance of an alpha- vs. beta-internal linkage. It was possible to unmask cryptic CFA-10 sites on pigeon (10-) RBC's with use of specific glycosidases. While these cryptic sites also were susceptible to alpha-galactosidase, they may not be identical to the naturally exposed CFA 10 sites on pigeon (10+) RBC's. When pigeon (10-) RBC's were incubated in vitro with serum from 10+ pigeons, CFA 10 was detectable on the RBC surface. It is suggested that one mechanism of controlling the presence of CFA 10 on pigeon RBC's may be developmental changes in gene expression mediated through the serum environment.
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PMID:Identification of a galactose-like component of a chicken onco-developmental antigen. 616 57

Six glycoside hydrolases in the culture medium of Bacteroides fragilis--alpha-glucosidase, beta-glucosidase, alpha-galactosidase, beta-galactosidase, beta-N-acetylglucosaminidase, and alpha-L-fucosidase-were systematically purified by ammonium sulfate precipitation, gel filtration chromatography, and density gradient isoelectric focusing. The isoelectric focusing resolved the glycosidases into distinct, well-separated fractions and revealed three differently charged forms of beta-N-acetylglucosaminidase and of alpha-L-fucosidase. Furthermore, alpha-glucosidase and beta-N-acetylglucosaminidase were shown to possess dual affinities for the respective galactoside substrates, and beta-galactosidase also hydrolyzed beta-D-fucoside. alpha-Glucosidase was purified to homogeneity, as indicated by a thin-layer isoelectric focusing zymogram technique. The glycosidases, with exception of beta-glucosidase and the acid alpha-L-fucosidase, were each separated from other glycosidic activities to 99%. The molecular weights varied between 58,000 and 125,000. The pH optima ranged from 4.8 to 6.9.
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PMID:Purification of glycoside hydrolases from Bacteroides fragilis. 625 Apr 77

A study of three lysosomal enzymes (hexosaminidase, beta-galactosidase and alpha-galactosidase) in normal primary amniotic fluid cell cultures using a microenzymatic assay is presented. No difference in enzyme activity was found between primary and amniotic cell cultures in passage number one. A progressive change in the proportions of hexosaminidase A and hexosaminidase B with time was demonstrated in culture. The feasibility of this procedure for the early prenatal diagnosis of disorders due to lysosomal enzyme deficiency is discussed.
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PMID:Microenzymatic assays for lysosomal enzymes in primary amniotic fluid cell cultures. 625 Jul 42

The developmental patterns of four lysosomal enzymes have been investigated in liver, kidney, lung, heart, spleen, muscle and brain tissues of human fetuses at varius gestational ages. The largest increment in the activity of all four enzymes, namely acid alpha-glucosidase, alpha-galactosidase, beta-galactosidase and acid phosphatase had been observed in kidney with a 6- to 12-fold increase between the second and third trimester of gestation. The activity of all liver and spleen enzymes also increased considerably during these periods. In muscle, however, only alpha-glucosidase and acid phosphatase showed an increase in the activity, and in lung, acid phosphatase and beta-galactosidase. Most of brain and heart enzymes, except acid phosphatase, did not change significantly during the observation period. The activities of these lysosomal enzymes were also measured in tissues of a normal adult individual, and aspects of the neonatal and postnatal development of these enzymes were discussed.
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PMID:Lysosomal enzyme activities of human fetal organs during development. 625 27

The condition for maximal activity (pH, buffer, saturating substrate concentration, range of linear relationships between enzyme activity versus incubation time, and versus enzyme concentration) in the fluorimetric assay of several glycohydrolases of lysosomal origin in human plasma and serum have been established. The following enzymes were studied: alpha-galactosidase, beta-galactosidase, beta-N-acetylglucosaminidase, beta-glucosidase, beta-glucuronidase, alpha-mannosidase, alpha-fucosidase. All examined enzymes turned out to be more or less unstable upon storage at 37 degrees C, 4 degrees c, and -20 degrees C in both serum and plasma. The only exceptions were beta-glucuronidase, which was stable in plasma and serum, and alpha-fucosidase which was stable only in plasma. Generally the degree of instability was greater in serum than in plasma. The levels of some enzymes (alpha-galactosidase, beta-galactosidase, beta-N-acetyl glucosaminidase, beta=glucuronidase) were markedly higher in serum than in plasma; conversely the levels of the same enzymes in "platelet free" serum equalled those in plasma. This stresses the necessity to use freshly prepared plasma for lysosomal glycohydrolase assay. Under the procedural conditions recommended for the assay the methods for the determination of lysosomal glycohydrolases in plasma appeared to be simple, sensitive and reproducible.
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PMID:Enzymes of lysosomal origin in human plasma and serum: assay conditions and parameters influencing the assay. 625 26

The enzyme activities of alpha-fucosidase (pH 4.0 and pH 5.5), alpha-galactosidase, beta-galactosidase, alpha-glucosidase (pH 4.5 and pH 6.0), beta-glucosidase, beta-glucuronidase, beta-hexosaminidase, and alpha-mannosidase (pH 4.5 and pH 5.5) were investigated in sera from cystic fibrosis (CF) patients. Several of these activities were significantly increased in sera from patients compared to age-matched control children. CF-patients in a more advanced stage of the disease had a tendency to higher values of some of these hydrolases than those in better condition. No new isoenzymes of these hydrolases were found. Only minor differences could be detected in the pH-profiles of alpha-mannosidase and acid phosphatase from age-matched normal controls, heterozygotes and homozygotes for CF. With our technique, alpha-mannosidase and acid phosphatase showed the same thermostability in CF-patients. CF-heterozygotes and age-matched controls, except at 56 degrees C, when the activity of acid-phosphatase in the plasma from adult CF-heterozygotes decreased more than that from adult controls
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PMID:Acid hydrolases in sera and plasma from patients with cystic fibrosis. 626 20

The identification of female carriers of Fabry's disease is important for genetic counselling since prenatal diagnosis of affected fetuses is possible. The activities of either total alpha-galactosidase or alpha-galactosidase A in cultured fibroblasts were similar in Fabry carriers and controls and cannot therefore be used for carrier detection. Better discrimination between carriers and controls was found when total alpha-galactosidase activity was expressed as a ratio to beta-galactosidase activity, but overlap still occurred. However, there was complete discrimination between the ratio of alpha-galactosidase A to beta-galactosidase in cultured fibroblasts from five carriers of Fabry's disease and either 11 controls, seven hemizygote affected males or two of their female relatives.
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PMID:Fibroblast alpha-galactosidase A activity for identification of Fabry's disease heterozygotes. 627 49

In Fabry disease, as in other X-linked traits, identification of all heterozygotes is difficult. Reduced plasma alpha-galactosidase activities will correctly identify 60-70% of the carriers. The identification rate improves when an alpha/beta-galactosidase activity enzyme ratio is used. We measured alpha-galactosidase activity in reference to several other enzyme activities, beta-galactosidase, beta-hexosaminidase, and alpha-fucosidase in plasma and leukocytes from 22 suspected and 9 obligate carriers from 4 kindreds of Fabry disease patients. Utilizing such ratios or various combinations of ratios in plasma we have correctly identified the carrier state in 91% of heterozygotes. Leukocyte alpha/beta-galactosidase identified one more female than leukocyte alpha-galactosidase activities alone. We recommend the use of such multiple biochemical tests to identify carriers of Fabry disease.
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PMID:Heterozygote detection in Fabry disease utilizing multiple enzyme activities. 627 91


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