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The synthesis of polyesters and copolyesters containing the bicycl o[2. 2.2]octane ring and 1,4-cycl ohexanedi acetic acid and 1,4-cyclohexanedimethanol spacers are discussed. The following homopolyesters were synthesized: poly[oxy(2-methyll, 4-phenylene)oxycarbonyl-l,4-bicyclo[2.2.2]octylenecarbonyl] I; and poly[oxy(2-chloro-l,4-phenylene)oxycarbonyl-l,4-bicyclo[2.2.2]octy-1 enecarbonyl] II. The following copolyesters were synthesized: poly[oxy (2-chl oro- 1,4-phenyl ene )oxycarbonyl-l ,4-bi cycl o[2. 2. 2]octyl enecarbonyl-co-oxy- (2-chloro-1,4-phenylene)oxysebacoyl] III; poly[oxy(2-methyl-l,4- phenylene)oxycarbonyl-l,4-bicyclo[2.2.2]octylene-co-oxy(2-methyl-l,4- phenyl ene)oxysebacoyl] IV; poly[oxy(2-methyl-l,4-phenylene)oxyterephthaloyl- co-oxy(2-methyl-l,4-phenylene)oxy-l,4-cyclohexanediacetoyl] V; poly[oxy(2-methyl-1,4-phenylene)oxyterephthaloyl-co-oxymethylene-1,4 cyclohexylenemethyleneoxyterephthaloyl] VI; and poly[oxy(2-chloro-1,4 phenylene)oxyterephthaloyl-co-oxymethylene-1,4 cyclohexylenemethyleneoxyterephthaloyl]VII. The resulting homopolyesters and copolyesters were characterized by proton NMR, DSC, TGA, IR, solution viscosity, and polarizing optical microscopy.

Resultados de medidas de ponto de fusão, análise por raios-x e de espectroscopia infravermelho são apresentados para a identificação de dois polimorfos do ácido 5-etil-5-sec-butil barbitúrico (butabarbital).A estrutura do polimorfo II foi refinada simultaneamente com dois conjuntos de dados de origens diversas. Os dados cristalográficos são: a= 10,280 &#197, b= 20,091, c= 11,920, d= 110&#176 30\' monoclínico, grupo espacial I2/c, com oito moléculas por cela unitária.Os resultados obtidos com os dois conjuntos de dados concordam a menos do erro experimental. É comprovada a existência de desordem na estrutura e é feita uma análise dos problemas do refinamento. / Results of measures of melting point, X-ray analysis and infrared spectroscopy are presented for the identification of two polymorphs of acid 5-ethyl-5-sec-butyl barbiturate (butabarbital).The structure of polymorph II was refined simultaneously with two sets of data of different origins. The crystallographic data is a= 10,280 &#197, b= 20,091, c= 11,920, d= 110&#176 30\' monoclinic system, space group I2 / c with eight molecules per unit cell.The results obtained with the two data sets agree nothing experimental error. It neas proved the existence of disorder in the structure and on analyses done about the problems of refinement.

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Cataract is a leading cause of blindness throughout the world, yet the fundamental biochemical causes are unknown. A rodent model of the biochemical processes is selenite cataract. This cataract shows some of the features of human cataracts such as increased lens calcium, proteolysis of proteins, and insolubilization leading to lens opacity. The goals of the current experiments were: (1) To measure changes in transcript levels for calpains and caspase 3 and oxidation of epithelial proteins in selenite cataract. (2) To elucidate changes in calpain 10 and its interaction with other calpains in selenite cataract. (3) To investigate changes in stability of ��B1-crystallin caused by deamidation and truncation. These data would provide roles for apoptosis, protein insolubilization, proteolysis and deamidation observed in cataract. To induce cataract, 12-day old rats were injected with an overdose of Na���SeO���. Epithelium was analyzed by competitive RT-PCR, zymography, and thiol-blotting. Calpains were detected by western-blotting. For ��B1-crystallin stability studies, recombinant ��B1-crystallins were denatured by urea or heat. Urea stability was measured by circular dichroism and fluorescence spectrometry, and heat stability was measured by light scattering at 405 nm. During selenite cataract formation, calpains in epithelium were activated resulting in increased proteolysis of crystallins, but mRNA levels for calpains did not show appreciable changes. Oxidation of sulthydryls in epithelial proteins was minimal during cataract formation. These results suggested that calpain-induced proteolysis in the epithelium contribute to selenite cataract. In selenite cataract, calpain 10 proteins disappeared, which appeared to be due to degradation by calpain 2 and Lp82 calpain. Deamidated ��B1-crystallin was less stable in urea and heat, compared to wildtype. When the terminal extensions were removed, ��B1-crystallin was as stable as wild-type. However, without the extensions, truncated ��B1-crystallin caused accelerated precipitation in a complex with ��A-crystallin, suggesting that the extensions may contribute to proper association with other crystallins and to stability of the soluble complexes. In summary, proteolysis of proteins by calpains was more pronounced than protein oxidation in lens epithelium of selenite cataract. Deamidation and truncation caused instability of ��B1-crystallin and abnormal association with ��A-crystallin. Thus, proteolysis and deamidation may increase susceptibility of lenses to cataract. / Graduation date: 2003

The crystalline lens is a unique cellular organ that performs metabolic processes while maintaining optical functionality. Mitochondria play a vital role in providing the cell with the energy necessary for these metabolic processes and have recently been shown to be more metabolically active than previously thought. To test the hypothesis that mitochondrial function directly influences the optical function of the lens, bovine lenses were treated with 50 μM, 200 μM, 600 μM and 1000 μM menadione, a mitochondrial specific toxin that renders the mitochondria inactive, and the Back Vertex Distance (BVD) variability was observed over 216 hours. Confocal micrographs of secondary fibre cells’ mitochondria were also analyzed for 50 μM, 200 μM, and 600 μM menadione treatment over 48 hours. Increase in BVD variability (± s.e.m.) was observed within 24 hours from 0.28 ± 0.021 to 1.83 ± 0.75 for the 600 μM treated lenses. Confocal micrograph analysis showed a trend toward a decrease in the average length of mitochondria from 7.9 ± 0.8 to 3.7 ± 0.9 over for 200 μM treated lenses and from 5.9 ± 1.0 to 3.6 ± 0.6 for the 600 μM treated lenses over 48 hours. These data show that indeed menadione has a detrimental effect on mitochondria as a function of both time and concentration and this change in mitochondria precedes changes in BVD variability directly linking mitochondrial function to optical function.

The crystalline lens is a unique cellular organ that performs metabolic processes while maintaining optical functionality. Mitochondria play a vital role in providing the cell with the energy necessary for these metabolic processes and have recently been shown to be more metabolically active than previously thought. To test the hypothesis that mitochondrial function directly influences the optical function of the lens, bovine lenses were treated with 50 μM, 200 μM, 600 μM and 1000 μM menadione, a mitochondrial specific toxin that renders the mitochondria inactive, and the Back Vertex Distance (BVD) variability was observed over 216 hours. Confocal micrographs of secondary fibre cells’ mitochondria were also analyzed for 50 μM, 200 μM, and 600 μM menadione treatment over 48 hours. Increase in BVD variability (± s.e.m.) was observed within 24 hours from 0.28 ± 0.021 to 1.83 ± 0.75 for the 600 μM treated lenses. Confocal micrograph analysis showed a trend toward a decrease in the average length of mitochondria from 7.9 ± 0.8 to 3.7 ± 0.9 over for 200 μM treated lenses and from 5.9 ± 1.0 to 3.6 ± 0.6 for the 600 μM treated lenses over 48 hours. These data show that indeed menadione has a detrimental effect on mitochondria as a function of both time and concentration and this change in mitochondria precedes changes in BVD variability directly linking mitochondrial function to optical function.

In this research,we observed PAMA(poly(n-alkyl methacrylate)) and PAA(poly(n-alkyl acrylate)¡^side chain crystalline.We find side chain is longer and crystalize more easily,melting point is higher.In the result of DSC thermograms,the length of side chain is 6 carbons,we can't find any thermal transition.But the length of side chain is 12¡B18 carbons,we only found Tm.In PLM observation,we only get side chain crystalline's picture,and can't see any liquid crystalline yet. Although in X-ray's illustrative can find layer structure's diffraction peak,but i think this evidence can't prove the system that is liquid crystalline.It just can be said that the layed structure was formed by side chain crystallization.