Abstract
α-, β-, and γ-crystallins have been purified from nonpathological lenses of calves. The pure proteins have been examined for nontryptophan fluorescence and fluorescent compounds have been found specifically bound to γ 2-crystallin. The protein has been unfolded by 6 m guanidine hydrochloride (Gdn-HCl) and a separation of the fluorescent compounds has been obtained by gel chromatography in the presence of 6 m Gdn-HCl. The spectroscopic features (absorbance, fluorescence) of the protein returned to normal following removal of the chromophores. The low-molecular-weight separated fluorescent compounds have been fractionated and extracted from the Gdn-HCl solution by ethyl acetate. TLC chromatography has shown the presence of kynurenine, 3-OH-kynurenine, and free tryptophan. These data suggest that direct involvement of the intrinsic protein tryptophans in the photochemical processes leading to formation of fluorescent compounds has to be excluded. Free tryptophan and intrinsic metabolic factors are probably more relevant in determining the cataractous insult.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
