Loss of Free Amino Groups in the Water-insoluble Fraction of Nuclear Senile Cataracts

作者: M N Miranda-Rivera , S Garćia-Castiñeiras

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摘要: Free amino groups were analyzed in the water-insoluble fraction (WIF) of cataractous human lenses nuclear sclerosis, pigmented type. Two modified versions trinitrobenzene sulfonic acid (TNBS) procedure for determination free proteins (AFSA Habeeb, Anal Biochem 14:328-336, 1966) used this purpose. The concentration WIF was found to be inversely related dry weight fraction. Taking as a measure severity cataract, it can thus said that relative loss apparently occurs during insolubilization process associated type senile cataract. disappearance rate has been estimated about 0.9% — NH2 per 1 mg material added WIF. After considering other possible alternatives (loss accessibility TNBS, dilution by materials with low primary amine content) we have interpreted finding most likely due postsynthetic blockade lysine e-amino functions proteins. potential involvement residues Schiff base formation is discussed within context current views cataractogenesis. reaction e-NH2 unidentified carbonyl compounds could represent partial but quantitatively important mechanism yellowing cataracts. Invest Ophthalmol Vis Sci 24:1181-1187, 1983 Postsynthetic modifications are amply represented lens peculiarities its metabolism and growth. following described: racemization * 2 ; deamidation 34 oxidation sulphur 5 " 7 also probably aromatic aminoacids 8 glycosylation 9 polypeptide chain cleavage 310 disulfide nondisulfide cross-linking"" 13 appearance visible fluorescence. 14 18 We reporting new kind post-synthetic modification proteins, namely, which detected waterinsoluble Materials Methods

参考文章(34)
Rixon Kc, Harding Jj, Is diarrhoea a major cause of cataract in some tropical countries Metabolic and pediatric ophthalmology. ,vol. 5, pp. 161- ,(1981)
Antoinette Pirie, Color and solubility of the proteins of human cataracts Investigative Ophthalmology & Visual Science. ,vol. 7, pp. 634- 650 ,(1968)
H. Fraenkel-Conrat, J. Ieuan Harris, A. L. Levy, Recent Developments in Techniques for Terminal and Sequence Studies in Peptides and Proteins Methods of biochemical analysis. ,vol. 2, pp. 359- 425 ,(2006) , 10.1002/9780470110188.CH12
K.J. Dilley, Antoinette Pirie, Changes to the proteins of the human lens nucleus in cataract Experimental Eye Research. ,vol. 19, pp. 59- 72 ,(1974) , 10.1016/0014-4835(74)90073-6
L. Lorand, L. K. Hsu, G. E. Siefring, N. S. Rafferty, Lens transglutaminase and cataract formation Proceedings of the National Academy of Sciences of the United States of America. ,vol. 78, pp. 1356- 1360 ,(1981) , 10.1073/PNAS.78.3.1356
W. H. Garner, A. Spector, Racemization in human lens: evidence of rapid insolubilization of specific polypeptides in cataract formation. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 75, pp. 3618- 3620 ,(1978) , 10.1073/PNAS.75.8.3618
M. H. Garner, A. Spector, Selective oxidation of cysteine and methionine in normal and senile cataractous lenses Proceedings of the National Academy of Sciences of the United States of America. ,vol. 77, pp. 1274- 1277 ,(1980) , 10.1073/PNAS.77.3.1274
John F.R. Kuck, Nai-Teng Yu, Raman and fluorescent emission of the human lens. A new fluorophor. Experimental Eye Research. ,vol. 27, pp. 737- 741 ,(1978) , 10.1016/0014-4835(78)90045-3
Roger J.W. Truscott, Robert C. Augusteyn, Oxidative changes in human lens proteins during senile nuclear cataract formation Biochimica et Biophysica Acta. ,vol. 492, pp. 43- 52 ,(1977) , 10.1016/0005-2795(77)90212-4