Age-related changes in human lens crystallins identified by two- dimensional electrophoresis and mass spectrometry

Kirsten J. Lampi, Zhixiang Ma, Stacy R.A. Hanson, Misuyoshi Azuma, Marjorie Shih, Thomas (Tom) Shearer, David L. Smith, Jean B. Smith, Larry L. David

Research output: Contribution to journalArticlepeer-review

234 Scopus citations


The purpose of this study was to identify the major protein components in adult human lenses and to analyse the specific age-related changes in these proteins using two-dimensional electrophoresis, Edman sequencing, and in conjunction with the data in the accompanying manuscript, mass spectrometry. The majority of changes in the two-dimensional electrophoretic pattern of lens proteins occurred prior to 17 years of age, and included a decrease in proteins migrating to the original positions of βB1, βB3, βA3, γC and γD, and the appearance of many new species with apparent molecular weights on two-dimensional electrophoretic gels similar to βB2 and βS, but having more acidic pIs. These proteins were identified as deamidated forms of βB1 and βA3/A1 missing portions of their N-terminal extensions. With the exception of αB, deamidation was detected in all crystallin species. These data indicated that a major fraction of the water-soluble protein of the adult human lens is composed of truncated βB1 and βA3/A1 crystallins, and that nearly all human crystallins, including the β-crystallins, are susceptible to deamidation. The results also provided the most detailed map to date of the identities of protein species on two-dimensional electrophoresis gels of adult human lenses.

Original languageEnglish (US)
Pages (from-to)31-43
Number of pages13
JournalExperimental Eye Research
Issue number1
StatePublished - Jul 1998


  • Aging
  • Crystallins
  • Deamidation
  • Human
  • Lens
  • Mass spectrometry
  • Proteolysis
  • Two-dimensional electrophoresis

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience


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