Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

alpha-Galactosidase has been purified from Klebsiella Sp. No. PG-2, a bacterium isolated from rat small intestine, using calcium phosphate gel, DEAE-cellulose column chromatography and gel filtration technique. About 130-fold increase in specific activity was observed, the pH optimum of 6.5-7.0 characterizes the enzyme as neutral alpha-galactosidase. The optimum temperature was 37 degrees C and the energy of activation was 11,856 cal/mole. Km values obtained for raffinose, mellibose, stachyose and p-nitrophenyl-alpha-D-galactopyranoside were 20.0, 6.6 33.3 and 4.0 mM respectively. The activity was inhibited by p-CMB; iodoacetate, Ag2+, Hg2+, Cu2+, Pb2+ and galactose. Examination of the enzyme activity indicated that the enzyme is cytosolic and is inducible in nature.
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PMID:Purification and properties of alpha-galactosidase from Klebsiella Sp. No. PG-2. 216 19

Angiokeratoma corporis diffusum (ACD) is still often thought to be synonymous with Anderson-Fabry disease, a deficiency of alpha-galactosidase. It is important, however, to consider other possible enzyme deficiencies in patients with ACD. We report an 8-year-old boy with neurodevelopmental delay who was diagnosed as having fucosidosis following recognition of ACD in the dermatology department. Other cutaneous features in this patient included distal transverse purple nail bands, acrocyanosis and a naevus anaemicus. Histology and electron microscopy of skin papules was consistent with angiokeratoma. Skeletal survey demonstrated dysostosis multiplex. The diagnosis was confirmed by leucocyte oligosaccharide enzyme analysis. There are only three previous reports of fucosidosis in the U.K.
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PMID:Cutaneous manifestations of fucosidosis. 915 66

Hyperacute organ xenograft rejection can be prevented by removing anti-pig antibodies by extracorporeal absorption prior to transplantation. A novel recombinant absorber of anti-pig antibodies was developed by fusing the cDNA encoding the extracellular part of a mucin-type protein, P-selectin glycoprotein ligand-1, with an antibody Fc fragment cDNA, which upon coexpression with the porcine alpha1,3 galactosyltransferase carried the xenogeneic epitope, Galalpha1,3Gal (Liu J., Qian Y., Holgersson J., Transplantation 1997, 63, 1673-1682). The biochemical characterization of the mucin/Ig and its absorption efficacy compared with that of porcine thyroglobulin and Galalpha1,3Gal-conjugated beads are reported. The carbohydrate portion of the mucin/Ig constituted 43% of its molecular weight and the majority of the Galalpha1,3Gal epitopes were O-linked as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blotting following N-glycosidase F digestion. Gas chromatography-mass spectrometry of reduced and acetylated saccharides released by alpha-galactosidase treatment revealed that the fusion protein carried approximately 140 mol of terminal, alpha-linked galactose per mole protein. Based on the reduction in pig aortic endothelial cell cytotoxicity, Galalpha1,3Gal-substituted mucin/Igs on agarose beads were, on a carbohydrate molar basis, shown to be approximately 20 times more efficient than agarose-conjugated pig thyroglobulin, and approximately 5000 and 30,000 times more efficient than Galalpha1,3Gal-substituted agarose and macroporous glass beads, respectively. Structural features of the mucin backbone and its carbohydrate core saccharide chains determine the structural context, spatial orientation and spacing of Galalpha1,3Gal epitopes and are likely to explain the superior absorption efficacy of the recombinant mucin-type chimera.
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PMID:Multivalent Galalpha1,3Gal-substitution makes recombinant mucin-immunoglobulins efficient absorbers of anti-pig antibodies. 1258 48

Two forms of alpha-galactosidase (alpha-d-galactoside galactohydrolase, E.C. 3.2.1.22) which differed in molecular weight were resolved from Cucumis sativus L. leaves. The enzymes were partially purified using ammonium sulfate fractionation, Sephadex gel filtration, and diethylaminoethyl-Sephadex chromatography. The molecular weights of the two forms, by gel filtration, were 50,000 and 25,000. The 50,000-dalton form comprised approximately 84% of the total alpha-galactosidase activity in crude extracts from mature leaves and was purified 132-fold. The partially purified 25,000-molecular weight form rapidly lost activity unless stabilized with 0.2% albumin and accounted for 16% of the total alpha-galactosidase activity in the crude extract. The smaller molecular weight form was not found in older leaves.The two forms were similar in several ways including their pH optima which were 5.2 and 5.5 for the 50,000- and 25,000-dalton form, respectively, and activation energies, which were 15.4 and 18.9 kilocalories per mole for the larger and smaller forms. Both enzymes were inhibited by galactose as well as by excess concentrations of p-nitrophenyl-alpha-d-galactoside sub-strate. K(m) values with this substrate and with raffinose and melibiose were different for each substrate, but similar for both forms of the enzyme. With stachyose, K(m) values were 10 and 30 millimolar for the 50,000- and 25,000- molecular weight forms, respectively.
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PMID:Characterization of alpha-Galactosidase from Cucumber Leaves. 1666 11