Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro

Rao Gadiparthi, Edward Cotlier

Research output: Contribution to journalArticle

40 Citations (Scopus)

Abstract

When the human eye lens homogenate which was incubated with [14C]-acetylsalicylic acid (aspirin) and separated into α-, β-, and γ-crystallins by Sepharose 6B gel-filtration, the radiolabel was found in all the three crystallins. The significant decreases in the free ξ-amino groups of aspirin treated crystallins as compared to the untreated ones indicate the probable sites of acetylation in the crystallins: The inhibition of the binding of [14C]-glucose and [14C]-cyanate to the aspirin pre-treated crystallins suggests that prior acetylation with aspirin prevents the occurrence of the nonenzymatic glycosylation and carbamylation of the lens crystallins in vitro.

Original languageEnglish (US)
Pages (from-to)991-996
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume151
Issue number3
DOIs
StatePublished - Mar 30 1988
Externally publishedYes

Fingerprint

Glycosylation
Crystalline Lens
Crystallins
Aspirin
Lenses
Acetylation
Cyanates
Sepharose
Gel Chromatography
In Vitro Techniques
Gels
Glucose

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Aspirin prevents the nonenzymatic glycosylation and carbamylation of the human eye lens crystallins in vitro. / Gadiparthi, Rao; Cotlier, Edward.

In: Biochemical and Biophysical Research Communications, Vol. 151, No. 3, 30.03.1988, p. 991-996.

Research output: Contribution to journalArticle

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