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α-Galactosidase ( EC 3.2.1.22, α-GAL, α-GAL A; systematic name α-D-galactoside galactohydrolase) is a glycoside hydrolase enzyme that catalyses the following reaction: [1] Hydrolysis of terminal, non-reducing α- D -galactose residues in α- D -galactosides, including galactose oligosaccharides, galactomannans and galactolipids
A person who inherits this gene does not have enough of a functioning enzyme known as alpha-galactosidase A. The lack of alpha-galactosidase leads to Fabry disease. A deficiency of alpha-galactosidase A (a-GAL A, encoded by GLA) due to mutation causes a glycolipid known as globotriaosylceramide (abbreviated as Gb3, GL-3, or ceramide trihexoside ...
When the target gene is not found in the vector, the alpha fragment gene would be active, producing the alpha fragment and allowing for B-galactosidase to gain its activity. To trace the activity of B-galactosidase a colorless analog of lactose is used, X-gal. The hydrolysis of X-gal by B-galactosidase produces galactose, a blue colored compound.
Alpha-galactosidase (EC 3.2.1.22) (melibiase) [8] catalyzes the hydrolysis of melibiose into galactose and glucose. In man, the deficiency of this enzyme is the cause of Fabry's disease (X-linked sphingolipidosis). Alpha-galactosidase is present in a variety of organisms.
There is no indication that a dog with this type of cancer could avoid surgery. If the tumor is small and can be removed completely, the dog will have a much better prognosis. If surgery is not an ...
Dogs can develop carcinomas of epithelial cells and organs, sarcomas of connective tissues and bones, and lymphomas or leukemias of the circulatory system. Selective breeding of dogs has led certain pure-bred breeds to be at high-risk for specific kinds of cancer. [1] Veterinary oncology is the medical study of cancer in animals, and can be ...
Capsular-polysaccharide endo-1,3-α-galactosidase (EC 3.2.1.87, polysaccharide depolymerase, capsular polysaccharide galactohydrolase) is an enzyme with systematic name Aerobacter-capsular-polysaccharide galactohydrolase. [1] [2] It catalyses random hydrolysis of (1→3)-α-D-galactosidic linkages in Aerobacter aerogenes capsular polysaccharide.
Two recombinant enzyme replacement therapies are available to functionally compensate for α-galactosidase deficiency. Agalsidase α and β are both recombinant forms of the human α-galactosidase A enzyme and both have the same amino acid sequence as the native enzyme. Agalsidase α and β differ in the structures of their oligosaccharide side ...
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