Liberation of N-acetylglucosamine-6-sulfate by human beta-N-acetylhexosaminidase A.
نویسندگان
چکیده
منابع مشابه
N-acetylglucosamine-6-sulfate sulfatase deficiency reconsidered.
design (3). We can imagine that some statistical procedure more powerful than standard Mantel-Haenszel and Miettinen tests might narrow the confidence intervals a bit, but it would not alter these point estimates by much. Adjustment of the RR's for tobacco use provides an adequate test for confounding. With subjects categorized either as non-, ex-, or current cigarette smokers or as pipe or cig...
متن کاملN-Acetylglucosamine-6-sulfate sulfatase from human urine.
N-Acetylglucosamine-6-sulfate sulfatase, which liberates sulfate from the N-acetylglucosamine 6-sulfate residue at the nonreducing terminus of a 3H-labeled trisaccharide prepared from heparan sulfate, was purified 136-fold from human urine. The final N-acetylglucosamine-6-sulfate sulfatase preparation was free of all lysosomal sulfatases known to act on sulfated polysaccharides and gave a singl...
متن کاملDistinguishing Candida species by beta-N-acetylhexosaminidase activity.
A variety of fungi produce the hydrolytic enzyme beta-N-acetylhexosaminidase (HexNAcase), which can be readily detected in assays by using p-nitrophenyl-N-acetyl-beta-D-glucosaminide as a substrate. In the present study we developed a microtiter plate-based HexNAcase assay for distinguishing Candida albicans and Candida dubliniensis strains from other yeast species. HexNAcase activity was detec...
متن کاملStabilization of human beta-D-N-acetylhexosaminidase A towards proteolytic inactivation by coupling it to poly(N-vinylpyrrolidone).
Human hexosaminidase A was covalently bound to soluble poly(N-vinylpyrrolidone), and the effect of this binding on the enzyme inactivation by various procedures was investigated. Whereas the polymer-bound hexosaminidase underwent inactivation to the same extent as the free enzyme, when exposed to heat or acidic pH, the conjugation to polymer appeared to protect the enzyme towards proteolysis. T...
متن کاملPurification, characterization, and cloning of a Spodoptera frugiperda Sf9 beta-N-acetylhexosaminidase that hydrolyzes terminal N-acetylglucosamine on the N-glycan core.
Paucimannosidic glycans are often predominant in N-glycans produced by insect cells. However, a beta-N-acetylhexosaminidase responsible for the generation of paucimannosidic glycans in lepidopteran insect cells has not been identified. We report the purification of a beta-N-acetylhexosaminidase from the culture medium of Spodoptera frugiperda Sf9 cells (Sfhex). The purified Sfhex protein showed...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1981
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)42985-7