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1.
Neutron irradiation of Cp2MoCl2 for 24 h afforded the radiotracer Cp299MoCl2 which was characterised by UV–Vis spectroscopy and thin layer chromatography. Binding experiments with the thiol containing protein human serum albumin (HSA) or calf thymus DNA, were monitored for 99Mo using a gamma counter. Under the conditions investigated, molar ratios of binding of 0.2:1 (Cp2MoCl2:DNA) and 9.4:1 (Cp2MoCl2:HSA) were calculated. The results are consistent with in vitro coordination studies that have shown strong preferential interaction of Cp2MoCl2 with thiols versus other donor sites in biomolecules including DNA. 相似文献
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Oxidation of cysteine, glutathione and ascorbate by photoexcited proteins from normal and cataractous lenses was investigated using electron paramagnetic resonance in combination with spin trapping. We report that illumination of these proteins in pH 7 buffer with light > 300 nm in the presence of thiols (RSH) and a spin trap 5,5-dimethyl-1-pyrroline N-oxide (DMPO), afforded DMPO/S-cysteine and DMPO/SG adducts, suggesting the formation of the corresponding thiyl radicals. In a nonbuffered aqueous solution, illumination of the proteins and glutathione also produced superoxide detected as a DMPO/O2H adduct. Irradiation of these proteins in the presence of ascorbate generated ascorbate radical. We conclude that chromophores present in the natural normal and cataractous lenses are capable of initiating photooxidative processes involving endogenous thiols and ascorbic acid. This observation may be pertinent to UV-induced development of cataract. 相似文献
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Abstract Porphyrins, which may be introduced into the eye as a result of abnormal porphyrin metabolism (uroporphyrin–Uro) or when used in the diagnosis or photodynamic therapy of certain tumors, including intraocular tumors (hematoporphyrin–Hp and'hematoporphyrin derivative'–Hpd and mesotetra( P -sulfonatophenyl)porphyrin–TPPS) are efficient photosensitizers in biological systems. We have been studying the potential phototoxic side effects of these drugs in the lens of the eye. Encapsulated in the human lens is a mixture of soluble protein crystallins. With little turnover of protein in the lens, any photosensitized modifications will accumulate and may result in an opacification of the lens. To evaluate the potential of different porphyrins to induce such damage, a series of porphyrins were photolyzed (transmission above 295 nm) in the presence of calf lens protein (2 mg m−1 ). Marked photopolymerization and histidine destruction were observed for the lens protein photolyzed in the presence of all of the drugs. We have found that the relative effectiveness of the following porphyrins to induce that damage is: Uro = TPPS Hpd = Hp. Both the singlet oxygen quencher, azide, and the free radical scavenger, penicillamine, decrease this photosensitized oxidative damage to lens protein. TPPS binds significantly to lens protein and this binding leads to conformational changes in that protein. 相似文献
5.
Strachan JD Adler H Alling P Ancher C Anderson H Anderson JL Ashcroft D Barnes CW Barnes G Batha S Bell MG Bell R Bitter M Blanchard W Bretz NL Budny R Bush CE Camp R Caorlin M Cauffman S Chang Z Cheng CZ Collins J Coward G Darrow DS DeLooper J Duong H Dudek L Durst R Efthimion PC Ernst D Fisher R Fonck RJ Fredrickson E Fromm N Fu GY Furth HP Gentile C Gorelenkov N Grek B Grisham LR Hammett G Hanson GR Hawryluk RJ Heidbrink W Herrmann HW Hill KW Hosea J Hsuan H Janos A Jassby DL Jobes FC 《Physical review letters》1994,72(22):3526-3529
6.
de la Vaissiere C Luth V Abrams GS Amidei D Baden AR Barklow T Boyarski AM Boyer J Breidenbach M Burchat P Burke DL Butler F Dillon JW Dorfan JM Feldman GJ Gidal G Gladney L Gold MS Goldhaber G Golding LG Hanson G Haggerty J Herrup D Himel T Hollebeek RJ Innes WR Jaros JA Juricic I Kadyk JA Klein SR Lankford AJ Larsen RR LeClaire BW Levi ME Lockyer NS Matteuzzi C Nelson ME Ong RA Perl ML Richter B Ross MC Rowson PC Schaad T Schellman H Schmidke WB Sheldon PD Trilling GH Yelton JM Wood DR 《Physical review letters》1985,54(19):2071-2074
7.
Joan E. Roberts Stephen J. Atherton James Dillon 《Photochemistry and photobiology》1990,52(4):845-848
Previous studies have shown that mesotetra(p-sulfonatophenyl)porphine (TPPS) binds to lens proteins. This characteristic should increase the residence time of the sensitizer in the lens and therefore enhance the probability of inducing photooxidative damage to that tissue in vivo. Subsequent in vivo studies have verified that contention. The present studies were performed to determine the effect of such binding on the spectroscopy and photophysics of the porphyrins. It was found that the binding of TPPS (1) quenches the fluorescence of lens proteins, (2) causes a shift in the ground state absorption spectra, fluorescence excitation spectra and the triplet excited state spectrum of TPPS to longer wavelengths and (3) results in an increase in the triplet state lifetime of TPPS. In the presence of the isolated crystallins the average triplet lifetime increases in the following order: gamma less than beta less than alpha. 相似文献
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