Immunochemical Relationship between Soluble and Insoluble Lens Proteins

1970 ◽  
Vol 1 (1) ◽  
pp. 10-20 ◽  
Author(s):  
P.D. Mehta ◽  
S. Lerman
Keyword(s):  
Lens Proteins ◽  
Immunochemical Relationship

scholarly journals Simultaneous and Rapid Detection of Multiple Epimers and Isomers of Aspartyl Residues in Lens Proteins Using an LC-MS-MRM Method

ACS Omega ◽  
2020 ◽  
Vol 5 (42) ◽  
pp. 27626-27632
Author(s):  
Noriko Fujii ◽  
Takumi Takata ◽  
Ingu Kim ◽  
Toshiya Matsubara
Keyword(s):  
Rapid Detection ◽  
Lens Proteins

scholarly journals Reaction of tyrosine oxidation products with proteins of the lens

1968 ◽  
Vol 109 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Antoinette Pirie
Keyword(s):  
Ascorbic Acid ◽  
Fluorescence Spectra ◽  
Ferrous Sulphate ◽  
Oxidation Products ◽  
Thiol Groups ◽  
Lens Proteins ◽  
Bovine Lens ◽  
Tyrosine Oxidation ◽  
Cataractous Lens

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.

Glycosylation of lens proteins in senile cataract and diabetes mellitus

1984 ◽  
Vol 123 (3) ◽  
pp. 888-893 ◽  
Author(s):  
Jin H. Lee ◽  
Dong H. Shin ◽  
Aaron Lupovitch ◽  
Dian X. Shi
Keyword(s):  
Diabetes Mellitus ◽  
Senile Cataract ◽  
Lens Proteins
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