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. 1978 Mar;75(3):1204–1208. doi: 10.1073/pnas.75.3.1204

Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from normal human lenses and cataracts.

P M Masters, J L Bada, J S Zigler Jr
PMCID: PMC411438  PMID: 274711

Abstract

High D/L aspartic acid ratios are observed in heavy molecular weight aggregates and in water-insoluble protein extracted from whole lenses and nuclear and cortical regions. Purified alpha-, beta-, and gamma-crystallins have low D/L ratios. Fractionation of urea-solubilized material from the water-insoluble protein yields four molecular weight classes of proteins. Fractions representing crosslinked material or apparently degraded products have high D/L ratios. Racemization within lens proteins may contribute to formation of the water-insoluble fraction seen in aging lenses and cataracts.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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