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Glucosaminidase

The effect of lactone ring-size on the inhibition was studied, for N-acetyl-)3-D-glucosaminidase from bovine epididymis, with lactones and lactone derivatives unable to undeigo ring-isomerization, by Pokomy and co-workers. From a comparison of Kj values for 2-acetamido-2-deoxy-D-glu-cono-1,5-lactone (0.45 nM) with the 1,4-lactone (4.5 fiM) and of Kj for the methyl ) -furanoside with that for the pyranose (4 mM), it was concluded that the 1,4-lactone has an 10-fold lower inhibitory potency than the 1,5-lactone. The weak inhibition by the 5,6-O-isopropylidene derivative of the... [Pg.330]

Brogren CH, Christensen JM, Rasmussen K. 1986. Occupational exposirre to chlorinated organic solvents and its effect on the renal excretion of N-acetyl-beta-D-glucosaminidase. Arch Toxicol Suppl 9 460-464. [Pg.255]

Monitoring of Cd exposure can take place by the determination of Cd in whole blood (reflects recent exposure) or urine (reflects body burden) by GF-AAS. Early effects can be monitored by the determination of a tubular protein (e.g. 132-microglobulin, retinol binding protein, a2-microglobulin) or the activity of an enzyme (e.g. N-acetyl 3-D-glucosaminidase) in urine. [Pg.204]

Alkaline conditions are used so frequently in carbohydrate separations on CarboPac columns that it should be pointed out that acidic conditions are suitable for separation of acidic sugars. Figure 24 shows the separation of sialic acid containing oligosaccharides.256 Alkaline conditions were used for neutral milk oligosaccharides and mucin oligosaccharide alditols were characterized similarly.257 The carbohydrates released from yeast mannopro-tein with N-acetyl-P-D-glucosaminidase were also fractionated on CarboPac ... [Pg.253]

Chia KS, Mutti A, Tan C, et al. 1994. Urinary N-acetyl-D-glucosaminidase activity in workers exposed to inorganic lead. Occup Environ Med 51 125-129. [Pg.501]

Sanfilippo B MPS IIIB AT-acetyl-glucosaminidase Heparan sulfate... [Pg.686]

Since then it has been established that emulsin is a mixture of enzymes comprising in addition to /3-glucosidase28 the enzymes a-galactosidase, a-mannosidase, /3-glucuronidase and /3-(N-acetyl)-glucosaminidase. Concerning the process of purification of the Rohferment and the mode of differentiation of the constituent enzymes of emulsin, the most informa-... [Pg.74]

Minhas T and Greenman J (1989) Production of cell-bound and vesicle-associated trypsin-like protease, alkaline phosphatase and N-acetyl—glucosaminidase by Bacteroides gingivalis strain W50. J Gen Microbiol 135, 557-564. [Pg.55]

This enzyme [EC 3.2.1.52], also referred to as )3-hexos-aminidase and A-acetyl-/3-glucosaminidase, catalyzes the hydrolysis of terminal nonreducing Ai-acetylhexosamine residues in A-acetyl-/3-hexosaminides. A-Acetylgluco-sides and A-acetylgalactosides are substrates. [Pg.10]

C. T. Yuen, R. G. Price, P. F. G. Praill, and A. C. Richardson, A new and simple colorimetric assay procedure for IV-acetyl-P-D-glucosaminidase in urine,/. Clin. Chem. Biochem., 19 (1981) 884. (Abstr. XI Int. Congr. Clin. Chem.). [Pg.65]

I. Pocsi, S. A. Taylor, A. C. Richardson, K. H. Aamlid, B. V. Smith, and R. G. Price, VRA-GlcNAc Novel substrate for N-acetyl-P-D-glucosaminidase applied to assay of this enzyme in human urine, Clin. Chem., 36 (1990) 1884-1888. [Pg.67]


See other pages where Glucosaminidase is mentioned: [Pg.235]    [Pg.191]    [Pg.192]    [Pg.329]    [Pg.330]    [Pg.331]    [Pg.332]    [Pg.45]    [Pg.45]    [Pg.147]    [Pg.169]    [Pg.170]    [Pg.183]    [Pg.190]    [Pg.183]    [Pg.179]    [Pg.66]    [Pg.286]    [Pg.235]    [Pg.235]    [Pg.32]    [Pg.686]    [Pg.266]    [Pg.100]    [Pg.152]    [Pg.324]    [Pg.36]    [Pg.52]    [Pg.61]    [Pg.65]    [Pg.65]    [Pg.67]    [Pg.238]   
See also in sourсe #XX -- [ Pg.61 ]

See also in sourсe #XX -- [ Pg.61 ]




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A -Acetyl-P-glucosaminidase

A-Acetyl-p-D-glucosaminidase

Enzymes 3-glucosaminidase

Glucosaminidase Glucosidase

Glucosaminidase Lysozyme

Glucosaminidase N-acetyl

N-Acetyl P-D-glucosaminidase

N-Acetyl-P-D-glucosaminidases

N-Acetyl-b-D-Glucosaminidase

N-acetyl-beta-D-glucosaminidase

P-Glucosaminidase

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