Results 321 to 330 of about 18,981 (340)
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Pseudodeficiency of α‐galactosidase A

Clinical Genetics, 1982
Apparent deficiency of α‐galactosidase A was observed in a 51‐year‐old, clinically healthy male, with no clinical symptoms of Fabry disease, and without excess urinary excretion of ceramide trihexoside. The deficiency, which was similar to that found in Fabry disease patients, could be demonstrated using both synthetic and natural substrates.
Eliezer Rosenmann   +3 more
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Glucosidases and galactosidases in soils

Soil Biology and Biochemistry, 1988
Abstract An improved method to assay activities of α- and β-glucosidases and α- and β-galactosidases in soils is described. It involves extraction and colorimetric determination of the p-nitrophenol released when 1 g of soil is incubated with 5 ml of buffered p-nitrophenyl glycoside solution at 37°C for 1 h.
F. Eivazi, M. A. Tabatabai
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[34] β-Galactosidase

1974
Publisher Summary The enzyme β-galactosidase is one of several oligosaccharide-splitting enzymes that have been purified and subsequently characterized to varying degrees both physically and mechanistically. It is found in a wide range of biological sources in both the plant and animal kingdoms, although the principal source of study has been in the ...
Edward Steers, Pedro Cuatrecasas
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20 β-Galactosidase

1972
Publisher Summary This chapter presents information on the chemistry and enzymology of β-galactosidases. β-Galactosidases have been found in numerous microorganisms, animals, and plants. Tests for fermentation of lactose play an important role in diagnostic bacteriology of Enterobacteriaceae, so the occurrence of β-galactosidase in gram-negative rods
Kurt Wallenfels, Rudolf Weil
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[33] α-Galactosidase

1974
Publisher Summary The α-galactosidase from the coffee bean is one of the few capable of hydrolyzing the nonreducing terminal α-D-galactopyranosyl residue of blood group B antigens. As part of the studies on the structure of these antigens in human erythrocytes, a method has been developed for the rapid and complete purification of the enzyme in high ...
H. M. Flowers, Noam Harpaz
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Beta-Galactosidase of Helix pomatia

Nature, 1964
THE 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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Hydrophobic chromatography of β‐galactosidase

Biotechnology and Bioengineering, 1980
AbstractThe hydrophobic interaction of β‐galactosidase with Sepharose 4B substituted with 3,3′‐diaminodipropylamine was studied in both batch and column experiments. The equilibrium and the binding rate constants were determined for different phosphate buffer concentrations.
R. G. Carbonell   +2 more
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Beta-Galactosidase Staining in the Skeleton

2014
The 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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Galactosidases from Aspergillus niger

Archives of Biochemistry and Biophysics, 1970
Abstract α- And β- d -galactopyranosidases were purified from a commercial crude enzyme preparation (Rhozyme HP-150). Although both enzymes were still not homogeneous, they were free of other possibly interfering glycosidases. Properties of the purified enzymes were studied.
Victoria Wacek, Yuan C. Lee
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β-Galactosidase Assay

Cold Spring Harbor Protocols, 2010
INTRODUCTIONWhen a transient or stable transfection assay is developed for a promoter, a primary objective is to quantify promoter strength. Because transfection efficiency in such assays can be low, promoters are commonly fused to heterologous reporter genes that encode enzymes that can be quantified using highly sensitive assays. The reporter protein’
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