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 effects of age-specific peculiarities and the duration of maintaining rats on a ration with 4 per cent of protein (the initial mass of rats in the 1st group 100 g each; duration of the experiment--30 days. Initial mass rats in the 2d group--200 g each; duration of experiment--90 days on the activity of the lysosomal hydrolase was studied. The latter included beta-glucosidase, beta-galactosidase, beta-glucoronidase, beta-N-acetylglucosaminidase, arylsulfatase A and B, acid phosphatase, phospholipase A1 and A2, cholinesterase, the total proteolytic activity and that of catepsines A, B, C and D. An ambiguity of changes in the enzymes activity in the animals of the 1st and 2d groups was revealed. Placing the growing animals on a ration containing 4 per cent of protein produces an activation of the most of the lysosomal enzymes, whereas in animals of the 2d test group the nature of changes in the activity of individual enzymes proved to differ quite appreciably. Thus, the summary activity of catepsines, beta-glucoronidase and cholinesterase was below the control level, while the activity of beta-galactosidase, beta-N-acetyl-glucoseaminidase and phospholipase A1 and A2 went up. A prolonged maintenance of rats on a protein-poor ration led to upsetting the stability of the lysosomal membranes, which manifested itself in a higher solubilization of lysosomal enzymes in vitro.
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PMID:[Characteristics of the enzymatic adaptation of rat liver lysosomes to protein deficiency]. 68 19

Excess of vitamin A induces decrease of neutral phospholipase A1 and A2 activity in rat testes homogenates on the 4th day, and increase of beta-galactosidase activity on the 8th day of treatment. It is suggested that phospholipase A activity decrease is of great importance in development of testicular disorders, caused by disbalance of vitamin A.
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PMID:Activity of phospholipases A and some lysosomal enzymes in rat testes at different stages of hypervitaminosis A. 70 51

A neutral sphingomyelinase which cleaves phosphorylcholine from sphingomyelin at a pH optima of 7.4 was purified 440-fold to apparent homogeneity from normal human urine concentrate employing Sephadex G-75 column chromatography, preparative isoelectric focusing, and sphingosylphospholcholine CH-Sepharose column chromatography. The enzyme is composed of a single polypeptide whose apparent molecular weight is 92,000. Analytical isoelectric focusing revealed that the pI of this enzyme is 6.5. Purified neutral sphingomyelinase was devoid of beta-galactosidase and beta-N-acetylglucosaminidase activity originally present in the urine concentrate. The purified neutral sphingomyelinase (N-SMase) had low levels of phospholipase A1 and A2 activity when phosphatidylcholine was used as a substrate and detergents were included in the assay mixture. However, it had no phospholipase activity toward phosphatidylglycerol and sphingomyelin at pH 4.5 irrespective of the presence or absence of detergents. Monospecific polyclonal antibodies raised against N-SMase immunoprecipitated approximately 70% of N-SMase activity from urine, human kidney proximal tubular cells, and partially purified membrane-bound N-SMase from these cells. Western immunoblot assays revealed that the monospecific polyclonal antibody against urinary N-SMase recognized both the urinary N-SMase and the membrane-bound N-SMase. Because this enzyme is distinct biochemically and immunologically as compared to acid sphingomyelinase (EC 3.1.4.12), we would like to assign it an enzyme catalog number of EC 3.1.4.13. The availability of N-SMase and corresponding antibody will be useful in studying various aspects of this enzyme in biological systems.
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PMID:Neutral sphingomyelinase from human urine. Purification and preparation of monospecific antibodies. 254 11

Lungs were obtained from rabbit fetuses (on each day from d 24 to d 30 of gestation), neonates and adults, and were fractionated for enzyme assays. The developmental profile of cytidylyltransferase shows a decrease in specific activity from d 25 to d 29 (P less than 0.05) then a sharp rise from d 30 to adult values in d 0 neonates (P less than 0.05). Cholinephosphotransferase specific activity changes little from d 25 to birth, apart from a non-significant peak on d 29. There is a sharp rise from neonatal d 0 to adult values on d 1 (P less than 0.01). The specific activity of microsomal phospholipase A2 declines from d 25 to reach adult values in the neonate (P = 0.05). In contrast, the specific activity of lysosomal phospholipase A2 rises from d 24-28 then falls in the neonate (P less than 0.05). Adult values are higher than those in the fetus and neonate. Three other lysosomal enzyme specific activities rise to d 28 then decline: phospholipase A1, beta-galactosidase, and beta-glucuronidase. The results demonstrate that the level of microsomal phospholipase A2 does not control the extent of remodelling of phosphatidylcholine for surfactant production. Lysosomal phospholipase A2 only increases in parallel with the other lysosomal enzymes, indicating an increase in the number of lysosomes in the lung.
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PMID:Developmental changes in enzyme activities in fetal and neonatal rabbit lung. Cytidylyltransferase, cholinephosphotransferase, phospholipases A1 and A2, beta-galactosidase, and beta-glucuronidase. 632 5