Characterization of Hyaluronidase 4 Involved in the Catabolism of Chondroitin Sulfate [PDF]
Molecules, 2022 Hyaluronidases (HYALs) are endo-beta-N-acetylhexosaminidases that depolymerize not only hyaluronan but also chondroitin sulfate (CS) at the initial step of their catabolism. Although HYAL1 hydrolyzes both CS and HA, HYAL4 is a CS-specific endoglycosidase.
Shuhei Yamada, Shuji Mizumoto
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Journal of Biological Chemistry, 1983 The two neutral beta-N-acetylhexosaminidases of rat brain have been purified by procedures involving extraction, concanavalin A-Sepharose, ammonium sulfate precipitation, DEAE-cellulose, hydroxyapatite, Sepharose 4B, and an affinity chromatography with 2-acetamido-N-(epsilon-aminocaproyl)-2-deoxy-beta-galactopyranosylamine bound to Sepharose.
T, Izumi, K, Suzuki
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Structural analysis of the carbohydrate chains of beta-N-acetylhexosaminidases from bovine brain. [PDF]
Biochem J, 1985 Overdijk B +9 more
europepmc +2 more sources
Degradation of keratan sulphate by beta-N-acetylhexosaminidases A and B. [PDF]
Biochem J, 1981 Ludolph T +3 more
europepmc +2 more sources
Affinity purification and subunit structures of beta-N-acetylhexosaminidases A and B from boar epididymis. [PDF]
Biochem J, 1984 Parkes HC, Stirling JL, Calvo P.
europepmc +2 more sources
Purification and characterization of an extracellular beta-n-acetylhexosaminidase from Paecilomyces persicinus [PDF]
Journal of Bacteriology, 1979 Both beta-N-acetylglucosaminidase nad beta-N-acetylgalactosaminidase activities were detected in the culture fluids of Paecilomyces persicinus P-10 after growth in a soybean meal-corn meal medium. The active material was purified by means of protamine sulfate fractionation and ultrafiltration, followed by ion exchange and gel chromatography.
L A, Eriquez, M A, Pisano
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BMC Evolutionary Biology, 2008 Background Beta-N-acetylhexosaminidases belonging to the glycosyl hydrolase 20 (GH20) family are involved in the removal of terminal β-glycosidacally linked N-acetylhexosamine residues.
Horner David S +2 more
doaj +1 more source
Purification and Characterization of .BETA.-N-Acetylhexosaminidase from Trichoderma harzianum.
Agricultural and Biological Chemistry, 1991 beta-N-Acetylhexosaminidase was produced by Trichoderma harzianum cultivated with chitin as the growth substrate. The enzyme was purified 13.2-fold to homogeneity by ultrafiltration and sequential chromatography on SP-Toyopearl and Sephacryl S-200. The molecular weight of the enzyme was estimated to be about 150,000 by gel filtration.
K, Koga +5 more
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Purification and characterization of .BETA.-N-acetylhexosaminidase from Penicillium oxalicum.
Agricultural and Biological Chemistry, 1985 β-N-Acetylhexosaminidase (EC 3.2.1.52) was purified from the culture filtrate of Penicillium oxalicum by fractionation with ammonium sulfate followed by successive column chromatographies with DEAE-cellulose, hydroxylapatite, Sephadex G-150 and Con A-Sepharose 4B. The purified enzyme was found to be homogeneous on polyacrylamide gel electrophoresis and
Kenji YAMAMOTO +3 more
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Purification and characterization of .BETA.-N-acetylhexosaminidase from Pycnoporus cinnabarinus.
Agricultural and Biological Chemistry, 1981 β-N-Acetylhexosaminidase (EC 3.2.1.52) was purified from the culture filtrate of Pycnoporus cinnabarinus to homogeneity by polyacrylamide disc gel electrophoresis. The ratio of β-GlcNAcase activity to β-GalNAcase activity remained constant during the purification process.
Akira OHTAKARA +3 more
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