| http://purl.uniprot.org/citations/6458607 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/6458607 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/6458607 | http://www.w3.org/2000/01/rdf-schema#comment | "The first step of the degradation of p-nitrophenyl-6-sulfo-2-acetamido-2-deoxy-beta-D-glucopyranoside and of keratan sulfate-derived oligosaccharides bearing N-acetylglucosamine-6-sulfate residues at the nonreducing end was considered to be accomplished by the action of a specific sulfatase (Kresse, H., Paschke, E., von Figura, K., Gilberg, W., and Fuchs W. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 6822-6826). In purification from human placenta, however, this activity co-chromatographed with isoenzyme A of beta-N-acetylhexosaminidase and had the same electrophoretic mobility as the latter enzyme. The activity was precipitated by a specific antiserum against beta-N-acetylhexosaminidase. A pronounced enzyme deficiency was found in Tay-Sachs and Sandhoff fibroblasts. The purified enzyme released p-nitrophenol from the chromogenic substrate as well as a second product which contained equimolar amounts of hexosamine and sulfate. This product had the same electrophoretic and chromatographic behavior as sulfated N-acetylglucosamine. It could be degraded by periodate to a smaller charged fragment. Incubation of keratan sulfate-derived oligosaccharides with beta-N-acetylhexosaminidase A analogously resulted in the liberation of N-acetylglucosamine-6-sulfate. The enzyme showed the highest affinity towards a trisulfated tetrasaccharide and exhibited a similar Km for the sulfated and the unsulfated p-nitrophenyl derivative."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)42985-7"xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/author | "Fuchs W."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/author | "Kresse H."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/author | "Glossl J."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/author | "Gilberg W."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/author | "Holtfrerich D."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/date | "1981"xsd:gYear |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/pages | "12926-12932"xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/title | "Liberation of N-acetylglucosamine-6-sulfate by human beta-N-acetylhexosaminidase A."xsd:string |
| http://purl.uniprot.org/citations/6458607 | http://purl.uniprot.org/core/volume | "256"xsd:string |
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