Enzymes 3-glucuronidase

Instead of myeloperoxidase as a marker enzyme, 3-glucuronidase, or elastase can be used with similar success. Myeloperoxidase measurement gives the fastest results, which might be important for doing additional HPLC the same day. 

Lin et al. (55,63) have described a method to lyse baker s yeast cells using subcritical and SCF CO2 (25-35°C, 7-34 MPa). In a batch process, pressurized CO2 was allowed to permeate the cells for a fixed time, followed by rapid depressurization. The rapid depressurization resulted in explosive expansion of the CO2 within the cells, leading to cell rupture and release of the cellular components. SCF CO2 at 35°C and 20 MPa was the most effective for enzyme release. Higher temperatures were more effective at cell disruption, but they also resulted in lower activity of the released enzymes. Enzyme release from baker s yeast cells was further enhanced with the addition of a cell-wall-lytic enzyme, (3-glucuronidase, to the cell mass before pressurization (55). 

Lysosomal enzymes (/3-glucuronidase, acid phosphatase, and deoxyribonuclease) w ere separated by differential centrifugation of Yoshida... 

Figure 5. Continued. Phagocytosis is indicated by the release of the lysosomal enzyme, -glucuronidase. Increased alveolar/capillary permeability is indicated by the increase in protein in the lavage fluid. (Reproduced with permission from ref. 22. Copyright 1988 Academic.)...

Spectrophotometric methods are, of course, not restricted to assays based on the NAD(P)+/NAD(P)H pair of coenzymes, and there are many natural and synthetic substrates whose reactions can be assayed in this way. The p-nitrophenyl group forms the basis of many convenient spectroscopic assays, for example for the enzyme glucuronidase ... 

There are several different types of hydrolytic reactions and enzymes car-boxylesterases, epoxide hydrolases, drug conjugate cleavage enzymes (glucuronidase, sulfatase, or phosphatase), and peptidases. The process of (3-oxidation described previously could also be considered a cleavage reaction. These reactions generally produce a metabolite that is more polar and susceptible to conjugation by Phase II enzymes. 

Enzymes, glucuronidases, and aryl sulfatases capable of splitting the conjugated products (glucuronates or sulfates) are found in a variety of animal tissues. These are acid hydrolases assumed to be associated with the lysosomal fraction. 

Cats also usually select only oral oils for inhalation. Cats do not have metabolic mechanism to break down essential oils due to the lack of the enzyme glucuronidase. Therefore, they should not be taken by mouth and should not be generally applied topically (Ingraham, 2008). 

Figure 4. Effect of hyperosmolality on lysosomal enzyme release from rabbit neutrophils. Cells were preincubated 10 min at 37 C in either regular HEPES buffer at 320 mosmol/kg ( ) or in HEPES buffer with 0.3-M sucrose at 680 mosmol/kg ( ), 5 Mg/mL cyto-chalasin B was added, cells were stimulated with FMLP, and p-glucuronidase was released into the medium during a 6-min period measured.

Figure 5. Inhibition of lysosomal enzyme release from neutrophils by increased osmotic strength. Cells were preincubated for 10 min at 37°C in regular buffer containing no additions (o), or containing sodium sulfate ( ), sodium HEPES ( ), or sucrose ( ) to increase the osmotic strength. Cells were treated with cyto-chalasin B (5 arid FMLP (10" M) and p-glucuronidase was...

Based on the data from animal studies, diisopropyl methylphosphonate is principally excreted in the urine as the metabolite IMPA (Hart 1976 Ivie 1980). Chromatographic behavior of urinary metabolites does not change after the urine is treated with glucuronidase and sulfatase, so there is no conjugation of diisopropyl methylphosphonate or IMPA by microsomal enzymes (Hart 1976). There was minimal excretion of diisopropyl methylphosphonate metabolites in bile (Hart 1976) or in the milk of a lactating cow (<1%) (Palmer et al. 1979). 

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-... 

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