Human α-Galactosidase A Mutants: Priceless Tools to Develop Novel Therapies for Fabry Disease. [PDF]
Modrego A +5 more
europepmc +1 more source
Human α-galactosidase A is stimulated by folic acid supplementation - possible implications in Fabry disease management. [PDF]
Khatoon S, Junaid MA.
europepmc +1 more source
Tri-Parametric Assessment of α-Galactosidase A Activity, lysoGb3 and X-Inactivation Aids Genotype-Phenotype Categorization of Fabry Disease Female Patients. [PDF]
Kuchar L +13 more
europepmc +1 more source
Identification and Characterization of a Thermostable GH36 α-Galactosidase from Anoxybacillusvitaminiphilus WMF1 and Its Application in Synthesizing Isofloridoside by Reverse Hydrolysis. [PDF]
Wang J, Cao X, Chen W, Xu J, Wu B.
europepmc +1 more source
Safety evaluation of an extension of use of the food enzyme α-galactosidase from the genetically modified <i>Saccharomyces cerevisiae</i> strain CBS 615.94. [PDF]
EFSA Panel on Food Enzymes (FEZ) +15 more
europepmc +1 more source
Plasma Globotriaosylsphingosine and α-Galactosidase A Activity as a Combined Screening Biomarker for Fabry Disease in a Large Japanese Cohort. [PDF]
Maruyama H +18 more
europepmc +1 more source
Expression, Purification, and Functional Exploration of an α-Galactosidase from <i>Akkermansia muciniphila</i>. [PDF]
Zuo T +6 more
europepmc +1 more source
Bioinformatics-Driven Multi-Factorial Insight into α-Galactosidase Mutations. [PDF]
Hay Mele B +5 more
europepmc +1 more source
α-D-Galactose-galactohydrolase (E.C.3.2.1.22), commonly referred to as α-galactosidase, catalyzes the hydrolysis of α-galactosidic linkages in oligo-saccharide such as raffinose, melibiose, stachyose and verbaschose. Legumes and its derivatives represent
Vidyavathi N +3 more
core
Isolation, Purification, and Characterization of α-galactosidase from Watermelon (Citrullus lanatus)
The enzyme α-galactosidase is a type of glycosidase that removes galactose sugar units from larger molecules in cells. Compounds that inhibit glycosidases have been useful for understanding the structure and function of the enzymes they inhibit, and some
Henley, Christopher, Jr.
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