Induction and efficient purification of endo-.ALPHA.-N-acetylgalactosaminidase from Alcaligenes sp.
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چکیده
منابع مشابه
Partial purification and characterization of an endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242.
For the purification of a new type of endo-alpha-N-acetylgalactosaminidase from the culture medium of Streptomyces sp. OH-11242 (endo-GalNAc-ase-S) [Iwase, Ishii, Ishihara, Tanaka, Omura & Hotta (1988) Biochem. Biophys. Res. Commun. 151, 422-428], a method for assaying enzyme activity was established. Using purified pig gastric mucus glycoprotein (PGM) as the substrate, oligosaccharides liberat...
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Exo-alpha-N-acetylgalactosaminidase has been purified 8000-fold from Clostridium perfringens by gel filtration, ion exchange chromatography, isoelectric precipitation, and negative adsorption on human O type erythrocytes. The resulting enzyme is active at physiological pH and temperature. Phenyl glycosides, oligosaccharides, mucins, glycolipids, and cell membranes are substrates for this enzyme...
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To cleave blood group A immunodeterminants from erythrocytes (Hoskins, L. C., Larson, G., and Naff, G. B. (1995) Transfusion 35, 813-821), we purified and characterized alpha-N-acetylgalactosaminidase (EC 3.2.1.49) activity from culture supernatants of the human fecal bacterium Ruminococcus torques strain IX-70. Three isoforms separated during hydrophobic interaction chromatography. Hydroxyapat...
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Two alpha-galactosidases (Ag-I & Ag-II) were purified from Acinetobacter sp. Both the enzymes were monomeric with pH optima of 7.0 and molecular weight of 65 kDa for Ag-I and 37 kDa for Ag-II. The temperature optima for Ag-I was between 50 and 60 °C and that of Ag-II was 40 °C. Both the enzymes were strongly inhibited by metal ions Ag2+ and Hg+, pCMB and SDS (1 %). The enzymes were found to be ...
متن کاملPurification and characterization of an endo-1,3-β-glucanase from Arthrobacter sp
An endo-1,3-β-glucanase from Arthrobacter sp. was purified by ammonium sulfate precipitation, anion-exchange and gel-filtration chromatographies. SDS/PAGE and gel-filtration chromatography suggested a monomer enzyme with molecular mass of 32,500. N-terminal sequence for 10 residues was APGDLLWSDE. Stable and optimum pHs were 5 to 8 and 6.5, respectively. Optimum temperature was 55°C , however, ...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1990
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.54.233