Dehydroalanine crosslinks in human lens

This study was conducted to develop a methodology for the purification and detection of histidinoalanine, lanthionine and lysinoalanine in the lens tissue. Cataractous and aged human lens proteins were hydrolysed and fractionated by using anion-exchange chromatography. The fraction containing the bu...

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Bibliographic Details
Published in:Experimental eye research 2004-10, Vol.79 (4), p.499-512
Main Authors: Linetsky, Mikhail, Hill, J.M.W., LeGrand, Roy D., Hu, F.
Format: Article
Language:English
Subjects:
Adult
Aged
Aging - metabolism
Alanine - analogs & derivatives
Alanine - analysis
Alanine - isolation & purification
cataract
Cataract - metabolism
Chromatography, High Pressure Liquid - methods
Chromatography, Ion Exchange - methods
Crystallins - analysis
Crystallins - isolation & purification
Dipeptides - analysis
Dipeptides - isolation & purification
histidinoalanine
Humans
lanthionine
Lens, Crystalline - chemistry
lysinoalanine
Lysinoalanine - analysis
Lysinoalanine - isolation & purification
Middle Aged
protein modification
Solubility
Sulfides
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Summary:This study was conducted to develop a methodology for the purification and detection of histidinoalanine, lanthionine and lysinoalanine in the lens tissue. Cataractous and aged human lens proteins were hydrolysed and fractionated by using anion-exchange chromatography. The fraction containing the bulk of dehydroalanine crosslinks was derivatized with dansyl chloride and then separated and quantified by means of RP-HPLC. The spectral and chromatographic properties of all three substances purified and quantified in this study were identical to those of their synthesized counterparts. Histidinoalanine and lanthionine were the most abundant dehydroalanine crosslinks in both water-soluble and water-insoluble lens proteins. Histidinoalanine levels in water-soluble proteins from the cataractous lenses of Indian origin were 6·2-fold higher than those in water-soluble proteins from normal lenses (1·68±0·75 vs 0·26±0·06 nmol/mg protein; p
ISSN:0014-4835
1096-0007
DOI:10.1016/j.exer.2004.06.026