Comparison between modifications of lens proteins resulted from glycation with methylglyoxal, glyoxal, ascorbic acid, and fructose

2002 ◽  
Vol 16 (3) ◽  
pp. 140-145 ◽  
Author(s):  
Mariana Argirova ◽  
Winrich Breipohl
Keyword(s):  
1968 ◽  
Vol 109 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Antoinette Pirie

Oxidation of tyrosine in the presence of bovine lens proteins leads to the formation of brown or black melanoproteins. Both tyrosinase and the oxidizing system of ferrous sulphate–ascorbic acid–EDTA are effective. The fluorescence of the lens proteins is both altered and enhanced by the tyrosine-oxidizing systems. Their fluorescence spectra resemble those of urea-insoluble proteins of human cataractous lens and of 1,2-naphthaquinone–proteins of naphthalene cataract. The lens proteins lose their thiol groups and, in acid hydrolysates of treated β-and γ-crystallins, a substance has been detected chromatographically that behaves similarly to a compound formed when 3,4-dihydroxyphenylalanine (dopa) is oxidized by tyrosinase in the presence of cysteine. Analysis and behaviour of this substance from hydrolysates of lens proteins suggest that it is a compound of cysteine and dopa.


1992 ◽  
Vol 1117 (2) ◽  
pp. 199-206 ◽  
Author(s):  
Simon H. Slight ◽  
Malladi Prabhakaram ◽  
Dong Bum Shin ◽  
Milton S. Feather ◽  
Beryl J. Ortwerth

Author(s):  
Mikhail Linetsky ◽  
Ekaterina Shipova ◽  
Rongzhu Cheng ◽  
Beryl J. Ortwerth

1995 ◽  
Vol 62 (3) ◽  
pp. 454-462 ◽  
Author(s):  
B. J. Ortwerth ◽  
Mikhail Linetsky ◽  
Paul R. Olesen

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