System mannitol

Another type of carbohydrate complex is the cyclic ester formed between a glycitol and a polyanion such as borate or molybdate (4). The possible species present at equilibrium have not previously been evaluated by iteration. The system mannitol-borate has been so analyzed, and it was possible to use the same approach as that for the metal chelates. 

Burger, C., Nguyen, F. N., Deng, J. and Mandel, R. J. (2005). Systemic mannitol-induced hyperosmolality amplifies rAAV2 mediated striatal transduction to a greater extent than local co-infusion. Mol. Ther. 11, 327-331. 

Chouvenc et al. (2004a) was compared with the predictions of the two previously quoted MTM models. The position of the sublimation interface and the thickness of the dry layer, denoted were estimated as functions of time by simple mass balances. Chouvenc et al. (2004a) observed that the Rp values derived from the three models were similar for < 6 mm and slightly lower than the few literature values. Moreover, experimental data correlation lines pass close to the axis origin, so that no significant crust effect was present in the experimentally investigated crystalline system (mannitol), in contrast to what is observed with concentrated vitreous systems that can present relatively large crust effects. 

Dissolution of 5 could be enhanced in H2O by solid dispersion systems with urea and mannitol (97MI27). A method for solubilizing 5 and 6 at near physiological pH was patented (98EUP856316). Solubility characteristics of 5 was investigated in an in vitro tear model (98MI24). 

S)-1,5-Anhydro-3,4,6-tri-0-benzyl-1 -C,2-0-(ophenylenemethylene)-D-mannitol Note. The isomeric chromene would be named as a 2-0,1 -C-substituted system. 

The Enzymes II (E-IIs) of the phosphoenolpyruvate (P-enolpyruvate)-dependent phosphotransferase system (PTS) are carbohydrate transporters found only in prokaryotes. They not only transport hexoses and hexitols, but also pentitols and disaccharides. The PTS substrates are listed in Table I. The abbreviations used (as superscripts) throughout the text for these substrates are as follows Bgl, jS-gluco-side Cel, cellobiose Fru, fructose Glc, glucose Gut, glucitol Lac, lactose Man, mannose Mtl, mannitol Nag, iV-acetylglucosamine Scr, sucrose Sor, sorbose Xtl, xylitol. 

However, observations early on indicated that the situation was more complicated because some systems, such as the mannitol PTS in E. coli lacked an E-III. Saier Jr. et al. [2] proposed that they might consist of an E-II with a covalently bound E-III, since the molecular weight of the E-II in these systems was comparable to that of E-II + E-III in the systems where they were found to be separate. A flurry of nucleotide sequence activity in the past several years has more than confirmed this prediction. 

Kinetic measurements on II reconstituted in proteoliposomes are also consistent with the phosphorylation without transport. Il reconstituted by the detergent dialysis method into proteoliposomes assumes a random orientation the cytoplasmic domains face inward for 50% and outward for 50%. Those facing inward catalyze transport of external mannitol to the interior when E-I, HPr and P-enolpyr-uvate are included on the inside. Those facing outward convert external mannitol to external Mtl-P when HPr, E-I and P-enolpyruvate are included in the external medium. Comparison of the rates showed that the rate of external phosphorylation in this system was higher than the rate of transport. If transport and phosphorylation were obligatorily coupled, the rate of phosphorylation would not exceed the rate of transport [70]. 

Fig. 10. Mechanisms of steady-slqte kinetics of sugar phosphorylation catalyzed by E-IIs in a non-compartmentalized system. (A) The R. sphaeroides 11 model. The model is based on the kinetic data discussed in the text. Only one kinetic route leads to phosphorylation of fructose. (B) The E. coli ll " model. The model in Fig. 8 was translated into a kinetic scheme that would describe mannitol phosphorylation catalyzed by Il solubilized in detergent. Two kinetic routes lead to phosphorylation of mannitol. Mannitol can bind either to state EPcy, or EPpe,. E represents the complex of SF (soluble factor) and 11 and II in A and B, respectively. EP represents the phosphorylated states of the E-IIs. Subscripts cyt and per denote the orientation of the sugar binding site to the cytoplasm and periplasm, respectively. PEP, phosphoenolpyruvate.

Fig. 6 DSC thermograms showing representative thermal transitions in frozen solutions. The top thermogram is for a mannitol solution and is characteristic of a metastable glass-forming system.

Figure 14 Observed permeability coefficients of urea and mannitol across monolayers of rat alveolar epithelial cells in primary culture in the Transwell system are correlated with transepithelial electrical resistance and days in culture.

Culture protocols have been published which describes an accelerated differentiation process where monolayers are ready to be used after 3-7 days of culture [90-92]. One of these systems, the so-called BD BioCoat Intestinal Epithelium Differentiation Environment, is commercially available through BD Bioscience. This system is described to produce monolayers of a quality that are comparable with the typical Caco-2 cells with respect to permeability for drugs transported transcellularly. The paracellular barrier function is however low, as indicated by high mannitol permeability and low TER. The functional capacity for active uptake and efflux is not as thoroughly characterized as for the standard Caco-2 mono-layers. 

Subsequent studies confirmed that there is no reliable evidence of the MPO-catalyzed hydroxyl generation by neutrophils [235,236]. Kettle and Winterbourn [237] demonstrated that the hydroxylation of salicylate by stimulated neutrophils or the purified MPO, which yielded 2,5-dihydroxybenzoate, was unaffected by hydroxyl radical scavengers mannitol or DMSO. These authors suggested that an active peroxidative agent in this system was the reduced Compound III, formed by the following reactions ... 

In 1977, Kellogg and Fridovich [28] showed that superoxide produced by the XO-acetaldehyde system initiated the oxidation of liposomes and hemolysis of erythrocytes. Lipid peroxidation was inhibited by SOD and catalase but not the hydroxyl radical scavenger mannitol. Gutteridge et al. [29] showed that the superoxide-generating system (aldehyde-XO) oxidized lipid micelles and decomposed deoxyribose. Superoxide and iron ions are apparently involved in the NADPH-dependent lipid peroxidation in human placental mitochondria [30], Ohyashiki and Nunomura [31] have found that the ferric ion-dependent lipid peroxidation of phospholipid liposomes was enhanced under acidic conditions (from pH 7.4 to 5.5). This reaction was inhibited by SOD, catalase, and hydroxyl radical scavengers. Ohyashiki and Nunomura suggested that superoxide, hydrogen peroxide, and hydroxyl radicals participate in the initiation of liposome oxidation. It has also been shown [32] that SOD inhibited the chain oxidation of methyl linoleate (but not methyl oleate) in phosphate buffer. 

The guanidino analogue 90 of the 7-membered cyclic urea system was prepared, enantiomerically pure, from D-mannitol. The derivative 90 selectively inhibits bovine kidney a-L-fucosidase at 2.8pM <00BMC307>. 

Different preparative procedures have been shown to yield protein fractions which are able to catalyze different types of reactions with respect to their requirement of either NAD or NADP as coenzymes [cf. Eqs. (19), (20), and (21)]. In sera of mice poisoned by carbon tetrachloride we found polyol dehydrogenases catalyzing the oxidation of the following polyols (a) with NAD sorbitol, ribitol, mannitol (b) with NADP sorbitol, ribitol. Erythritol and mt/o-inositol were not attacked at all. Figures 8 and 9 show the results of these determinations performed at pH 9.6. In the NAD system sorbitol and ribitol are oxidized at exactly the same rate, while in the NADP system ribitol does not reach the rate of sorbitol. The ratio NAD NADP for sorbitol is calculated to be 4.20 and for ribitol 5.50. Mannitol is oxidized at 23% of the rate of sorbitol. 

The stereochemistry of the hexitols affects the manner of ring fusion, as is seen in Figs. 3 and 4. In mannitol, sorbitol (gulitol) and iditol, the l,4 3,6-dianhydro rings are m-oriented, whereas in the dulcitol, allitol and altritol (talitol) series the 1,4 3,6-rings are trans-oriented. This makes the ring system in this latter series almost planar although in the case of dianhydrodulcitol and allitol there is considerable strain in the molecules. 

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