Oxidative modifications to crystallins induced in calf lenses in vitro by hydrogen peroxide.

Abstract:

:Calf lenses which are incubated in solutions of 1-150 mM H2O2 for 24 hr remain clear at 20 degrees C. While insoluble lens protein increases by at most 2-3%, we find extensive oxidation of exposed protein thiols, major shifts in the size distribution of crystallins, and progressive generation of more acidic polypeptides. Some of these oxidative modifications are reversible with reducing agent. beta H-Crystallins are particularly susceptible to oxidation: disulfide-bonded soluble aggregates form at low H2O2 levels, while irreversible dissociation to beta L-crystallins occurs at high H2O2 concentration. The gamma-crystallins are particularly prone to charge modification. In contrast, the size and charge distributions of alpha-crystallins appear to be virtually unaffected by H2O2.

journal_name

Exp Eye Res

authors

Siezen RJ,Coppin CM,Kaplan ED,Dwyer D,Thomson JA

doi

10.1016/s0014-4835(89)80072-7

subject

Has Abstract

pub_date

1989-02-01 00:00:00

pages

225-35

issue

2

eissn

0014-4835

issn

1096-0007

journal_volume

48

pub_type

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