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

Research output: Contribution to journalArticle

Abstract

High D/L aspartic acid ratios are observed in heavy molecular weight aggregates and in water-soluble protein extracted from whole lenses and nuclear and cortical regions. Purified α-, β-, and γ-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

Original languageEnglish (US)
Pages (from-to)1204-1208
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume75
Issue number3
DOIs
StatePublished - Jan 1 1978

ASJC Scopus subject areas

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