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Schematic representation of the design. Tryptophan metabolism is enriched in serum metabolites and gut microbiota of centenarians, potentially contributing to healthy longevity. A key tryptophan metabolite 5‐methoxyindoleacetic acid (5‐MIAA) is linked to the Christensenellaceae R‐7 group and exhibits effects of delaying cell senescence, promoting ...
Xiaorou Qiu+16 more
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Beta-Galactosidase of Helix pomatia
Nature, 1964THE digestive juice of Helix pomatia contains a remarkable number of enzymes; many of them are carbohydrases, and they include an enzyme that hydrolyses lactose or β-methyl-galactoside1,2. This communication describes the properties and activities of the enzyme that hydrolyses o-nitrophenyl-β-D-galactopyranoside (ONPG).
Got R, A Marnay, P Jarrige, J Font
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The discovery of β-galactosidase
Trends in Biochemical Sciences, 1989The enzyme beta-galactosidase was first mentioned in the literature by Beijerinck exactly a hundred years ago. The Department of Microbiology and Enzymology of the Delft University of Technology keeps the memory of Beijerinck, its first professor, alive by maintaining a 'Beijerinck-room' in the attic of the building.
Rouwenhorst, R.J. (author)+2 more
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Beta-Galactosidase Deficiency in the Hurler Syndrome
New England Journal of Medicine, 1969Abstract A deficiency of β-galactosidase (pH 5.0) was found in frozen tissues (brain, liver, kidney and spleen) from 10 patients with Hurler's syndrome (Types 1–3). The diminished activity of this enzyme was demonstrated with the use of nitrophenyl-galactosides as well as ganglioside GM1 and a "keratan sulfate-like" mucopolysaccharide.
Mae Wan Ho+6 more
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Immobilization of mold beta-galactosidase
Collection of Czechoslovak Chemical Communications, 1988We immobilized beta-galactosidase (EC 3.2.1.23) from the mold Aspergillus oryzae by various methods on the derivatives of bead cellulose manufactured by Czechoslovak industry. The activity, specific activity and operational stability of the immobilized enzyme were determined.
Alexandra Proskova+2 more
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Beta-Galactosidase Staining in the Skeleton
2014The lacZ gene, encoding for the β-galactosidase enzyme, is widely used as a reporter gene in bone biology due to the ease of visualization in situ on whole-mount or on tissue sections. In this protocol we provide detailed methods for visualizing this reporter gene for both in vivo and in vitro studies.
Jian Q. Feng, X. L. Han
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Generalized Gangliosidosis: Beta-Galactosidase Deficiency
Science, 1968A profound deficiency (10- to 30-fold) of β-galactosidase activity was found in tissues (liver, spleen, kidney, and brain) from two patients with generalized gangliosidosis; this deficiency is demonstrated as a failure to cleave both p -nitrophenyl-β-D-galactopyranoside and ganglioside GM 1 ...
Shintaro Okada, John S. O'Brien
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Three cases of beta-galactosidase deficiency
Klinische Pädiatrie, 1981A clinical description of three cases of beta-galactosidase deficiency is presented. Two cases are classical for infant type GM1-gangliosidosis, the third is characterised by dysostosis multiplex with growth retardation and of normal intelligence. Laboratory data revealed mucopolysaccharides in the urine of all described patients in a high level of ...
Ewa Pronicka+3 more
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Biochemistry, 1995
Human lysosomal beta-galactosidase is organized as a 680-kDa complex with cathepsin A (also named carboxypeptidase L and protective protein), which is necessary to protect beta-galactosidase from intralysosomal proteolysis. To understand the molecular mechanism of beta-galactosidase protection by cathepsin A, we defined the structural organization of ...
Marc-André Elsliger+3 more
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Human lysosomal beta-galactosidase is organized as a 680-kDa complex with cathepsin A (also named carboxypeptidase L and protective protein), which is necessary to protect beta-galactosidase from intralysosomal proteolysis. To understand the molecular mechanism of beta-galactosidase protection by cathepsin A, we defined the structural organization of ...
Marc-André Elsliger+3 more
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A dimer-dimer binding region in .beta.-galactosidase
Biochemistry, 1979alpha Complementation in beta-galactosidase is the restoration of enzyme activity by addition of the alpha donor CNBr2, from amino acid residues 3--92 of the polypeptide, to inactive M15 protein from the lacZ deletion mutant strain M15. M15 protein lacks residues 11--41 and is a dimer; the active complex, like native beta-galactosidase, is tetrameric ...
Irving Zabin, Franco Celada
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