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P-Glucosaminidase

Figure 29.7. Urinary excretion of proximal tubular enzymes following para-aminophenol (PAP) administration to female Sprague-Dawley rats. Rats received PAP (300mg/kgip) and urine was collected for 24 hr following treatment. Urine was assayed for activities of y-glutamyl transpeptidase (GGTP, O), trehalase (TRE, ), and A-acetyl-P-glucosaminidase (NAG, ). Data are expressed as a percentage of enzyme excretion in rats treated with saline. Each data point represents the mean standard error of at least four determinations. GGTP and TRE are enzymes located primarily on the brush border of proximal tubule cells, and NAG is an intracellular enzyme. Figure 29.7. Urinary excretion of proximal tubular enzymes following para-aminophenol (PAP) administration to female Sprague-Dawley rats. Rats received PAP (300mg/kgip) and urine was collected for 24 hr following treatment. Urine was assayed for activities of y-glutamyl transpeptidase (GGTP, O), trehalase (TRE, ), and A-acetyl-P-glucosaminidase (NAG, ). Data are expressed as a percentage of enzyme excretion in rats treated with saline. Each data point represents the mean standard error of at least four determinations. GGTP and TRE are enzymes located primarily on the brush border of proximal tubule cells, and NAG is an intracellular enzyme.
Endo-N-aoetyl-p-glucosaminidase F (Endo F) Flavobacterium meningosepticum 32 4-6 The other GIcNAc stays with the protein (like Endo H). ... [Pg.213]

FIGURE 23.28 HPLC profiles of the products obtained from exo-P-glucosaminidase hydrolysis of (GlcNlj-GlcNAc. The enzymatic reaction was performed in 50mM sodinm acetate bnffer, pH 5.0, at 37°C. Three microliters of the enzyme solution (0.5 jtM) was added to 100 i,L of the snbstrate solntion (10 mM). A portion of the reaction mixture was applied to a gel-filtration HPLC (TSK-GEL G2000PW), and eluted with 0.1 M NaCl with a flow rate of 0.3mol/min. [Pg.319]

Bossart and Bienz (1979) showed that poliovirus-infected enucleated HEp-2 cells exhibited the same cytopathic effect as poliovirus-infected nucleated cells. However, enucleated cells did not show the same redistribution of lysosomal enzymes (p-glucuronidase and p-glucosaminidase) into the cytoplasm as do infected nucleate cells however, it should be noted that enucleated cells do not support the replication of poliovirus as well as do nucleated cells. A temporal analysis of the events occuring in poliovirus-infected cells, as well as their cellular location, was made by Bienz et al. (1980). By kinetic analysis, viral protein synthesis was found to reach a maximum at 2.5 hr before cell alterations can even be detected. Poliovirus RNA synthesis reached a peak later (at 3.0-3.5 hr postinfection) when new vacuoles can be seen, although viral RNA synthesis continues as vacuoles coalesce to form the typical poliovirus cytopathic effect. Therefore, these authors consider that viral RNA synthesis and not protein synthesis is more closely related to structural changes possibly this could also include lysosomal structural changes. [Pg.45]


See other pages where P-Glucosaminidase is mentioned: [Pg.36]    [Pg.52]    [Pg.61]    [Pg.70]    [Pg.184]    [Pg.709]    [Pg.220]    [Pg.276]    [Pg.350]    [Pg.35]    [Pg.501]    [Pg.213]    [Pg.54]    [Pg.57]    [Pg.58]    [Pg.3510]    [Pg.314]    [Pg.318]    [Pg.3]    [Pg.46]   
See also in sourсe #XX -- [ Pg.35 ]

See also in sourсe #XX -- [ Pg.271 ]




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0- -glucosaminidase

A -Acetyl-P-glucosaminidase

A-Acetyl-p-D-glucosaminidase

N-Acetyl P-D-glucosaminidase

N-Acetyl-P-D-glucosaminidases

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