In vitro cross-linking of calf lens alpha-crystallin by malondialdehyde.
Int J Pept Protein Res
; 44(4): 342-7, 1994 Oct.
Article
in En
| MEDLINE
| ID: mdl-7875936
ABSTRACT
The effect of malondialdehyde on structural features of bovine alpha-crystallin has been investigated by absorption and fluorescence spectroscopy as well as by far-UV circular dichroism. Experimental evidence suggests the occurrence of intermolecular cross-linking induced by malondialdehyde. This cross-linking does not seem to affect the tryptophan environment, as suggested by intrinsic protein fluorescence. On the contrary, the time dependence of far-UV dichroic activity indicates that the cross-linking is accompanied by a secondary structure change. The formation of high molecular mass aggregates, evidence by electrophoresis in denaturing conditions, leads to irreversible alpha-crystallin aggregation due to extensive intermolecular cross-linking. Since malondialdehyde is produced in vivo as a breakdown product of lipid peroxidation the possible involvement of this molecule in the pathological mechanism of cataract formation has been briefly discussed.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Crystallins
/
Malondialdehyde
Limits:
Animals
Language:
En
Journal:
Int J Pept Protein Res
Year:
1994
Document type:
Article
Affiliation country:
Italy