Results 261 to 270 of about 14,424 (294)
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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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The formation of β-galactosidase in soil [PDF]
Folia Microbiologica, 1972 The activity of β-galactosidase during incubation of soil with lactose was studied. Enzyme activity reached its maximum between 6–24 h incubation. The addition of secondary ammonium phosphate stimulated the enzyme formation. Casein hydrolysate alone did not influence significantly enzyme formation even after a 72 h incubation.
P. Ryšavý, J. Macura
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Plasma α-galactosidase A: Properties and comparisons with tissue α-galactosidases
Biochimica et Biophysica Acta (BBA) - Enzymology, 1978The human plasma form of alpha-galactosidase A (alpha-D-galactoside galactohydrolase, EC 3.2.1.22) was highly purified and exhibited apparent Km values of 1.9 mM with 4-methylumbelliferyl-alpha-D-galactopyranoside and 0.23 mM with globotriglycosylceramide.
David E. Bishop, Charles C. Sweeley
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The assay of β-galactosidase in soil
Folia Microbiologica, 1972The method for the assay of β-galactosidase introduced by Lederberg (1950) was modified and used for studies of the enzyme in the soil.o-Nitrophenyl-β-d-galactoside served as substrate. Trismaleinate buffer was found to be more suitable than phosphate buffer in the assay.
P. Ryšavý, J. Macura
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Separation and properties of α-galactosidase and β-galactosidase from Cajanus indicus
Biochimica et Biophysica Acta (BBA) - Enzymology, 1974Abstract Cajanus indicus α- and β-galactosidase which are inseparable by Sephadex gel-chromatography (Dey, P. M. (1973) Biochim. Biophys. Acta 302, 393–398), have now been separated by CM-cellulose chromatography. α-Galactosidase (EC 3.2.1.22) has been resolved into two isoenzymes and β-galactosidase (EC 3.2.1.23) into three.
M. Dixon, Prakash M. Dey
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α-Galactosidase A in Vascular Disease
Trends in Cardiovascular Medicine, 2007Deficiency of alpha-galactosidase A (GLA) (Fabry disease) leads to the accumulation of glycosphingolipids in the vasculature leading to multiorgan pathology. In addition to well-described microvascular disease, deficiency of GLA is also characterized by premature macrovascular events such as stroke and possibly myocardial infarction.
James A. Shayman +2 more
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Inhibition of glucosidases and galactosidases by polyols
Archives of Biochemistry and Biophysics, 1966Abstract The hydrolyses of p-nitrophenyl α- and β-galactosides and p-nitrophenyl α- and β-glucosides by an α-galactosidase from Aspergillus fumigatis, an α-glucosidase from germinated barley, and almond β-glucosidase, which also has β-galactosidase activity, have been examined in the presence of glycerol, erythritol, d -threitol, ribitol, xylitol ...
Marianne V. Kelemen, W. J. Whelan
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Properties of mouse α-galactosidase
Biochimica et Biophysica Acta (BBA) - General Subjects, 1976alpha-Galactosidase has been examined in various murine tissues using the substrate 4-methylumbelliferyl-alpha-galactoside. Mouse liver appears to contain a single major form of the enzyme, as judged by chromatography and electrophoresis. The enzmye was purified 467-fold with a yield of about 40% by a method involving chromatography on Concanavalin A ...
Lusis, A J, Paigen, K
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On the mechanism of β-galactosidase induction
Archives of Biochemistry and Biophysics, 1961Abstract A 30-sec. pulse of tritiated leucine was given to logarithmically growing cells of Escherichia coli during induction with either melibiose or galactose. β-Galactosidase was thereafter isolated, and its specific radioactivity compared to that of the average cellular protein.
Barbara E. Wright, Gregory McNeil
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Endo‐β‐Galactosidases and Keratanase
Current Protocols in Molecular Biology, 1995AbstractThis overview covers the endo‐β‐galactosidases; enzyme is capable of hydrolyzing a wide range of glycoconjugates. Endo‐β‐galactosidases from numerous sources are discussed in terms of their substrate specificities and substrates, as well as their practical research applications.
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