RESUMO
We studied the in vitro digestion of lens crystallin by two fractions (Fractions A and B) of acidic lens-protein degrading activity from the bovine ciliary body. With whole lens crystallin as substrate, Fraction A degraded beta L-crystallin most significantly, and beta H-, gamma-, and alpha-crystallins moderately. Fraction B degraded alpha-crystallin most significantly, beta H- and beta L-crystallins moderately, and gamma-crystallin slightly. Insoluble protein was most resistant to digestion by Fractions A and B. Crystallins from the lens cortex and nucleus were degraded in the same manner as those from the whole lens.
Assuntos
Corpo Ciliar/metabolismo , Cristalinas/metabolismo , Ácidos/metabolismo , Animais , Bovinos , Fracionamento Químico , Cromatografia , Concentração de Íons de HidrogênioRESUMO
The level of ascorbate in the aqueous humor and surrounding intraocular structures in enucleated arterially perfused rabbit eye was investigated. The enucleated eye preparation was shown to be capable of secreting ascorbate from the perfusate into the aqueous humor. Ascorbate in the iris, ciliary body and cornea was released into the aqueous humor when the eye was perfused with ascorbate-free solution. Failure to obtain aqueous flow rates from the decay of ascorbate in the anterior chamber was due to the contribution of ascorbate from these ocular tissues during the perfusion. Histochemically, ascorbate was localized in the pigmented epithelial layer in the valleys between the ciliary processes and the pars plana of the ciliary body and in the iris. In the cornea, distinct localization of ascorbate was observed in the endothelium and basal cell layer of the epithelium.
Assuntos
Ácido Ascórbico/análise , Olho/análise , Animais , Humor Aquoso/análise , Corpo Ciliar/análise , Córnea/análise , Feminino , Histocitoquímica , Iris/análise , Cinética , Cristalino/análise , Masculino , Coelhos , Corpo Vítreo/análiseAssuntos
Cristalinas/análise , Ozônio/farmacologia , Idoso , Aminoácidos/análise , Congelamento , HumanosRESUMO
Four low molecular weight proteins (i.e. beta s, gamma H, gamma L1 & gamma L2 crystallins) were separated from the human cataractous lens cortex using gel filtration and chromatofocusing. Each of these four crystallins possessed its own subfractions in the pH gradient between 7.4 and 4.0 by chromatofocusing procedures. Analyses of the chromatofocusing patterns have further characterized the four crystallins. Polyacrylamide gel electrophoresis of these crystallin subfractions showed the possible separation of the heterogeneous protein bands.
