Literature DB >> 2924808

Racemization of aspartyl residues in proteins from normal and cataractous human lenses: an aging process without involvement in cataract formation.

P J van den Oetelaar1, H J Hoenders.   

Abstract

A highly sensitive method was used to determine D- and L-aspartyl residues in protein fractions from normal and cataractous human lenses. A linear relationship with age was found in all fractions from normal lenses. However, no correlation with cataract could be established. It is concluded that racemization of aspartyl residues is a continuous process in eye-lens proteins but plays no role in cataract formation.

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Year:  1989        PMID: 2924808     DOI: 10.1016/s0014-4835(89)80070-3

Source DB:  PubMed          Journal:  Exp Eye Res        ISSN: 0014-4835            Impact factor:   3.467


  2 in total

1.  Amino acid sequence of bovine gamma E (IVa) lens crystallin.

Authors:  G W Kilby; M M Sheil; D Shaw; J J Harding; R J Truscott
Journal:  Protein Sci       Date:  1997-04       Impact factor: 6.725

2.  Racemisation and human cataract. D-Ser, D-Asp/Asn and D-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses.

Authors:  Michelle Yu Sung Hooi; Roger J W Truscott
Journal:  Age (Dordr)       Date:  2010-08-05
  2 in total

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