Age-related changes in the polypeptide composition of β-crystallin from bovine lens

J. Samuel Zigler

Research output: Contribution to journalArticlepeer-review

Abstract

βH-Crystallin and βL-crystallin were isolated from bovine lenses of widely varying age. Electrophoretic analysis of the disaggregated polypeptide chains demonstrated marked age-related shifts in relative polypeptide abundance, both among the polypeptides common to βH and βL and those unique to βH. The data suggest the possibility that post-synthetic modifications may occur in bovine β-crystallin, as has previously been shown for bovine α-crystallin.

Original languageEnglish (US)
Pages (from-to)537-546
Number of pages10
JournalExperimental eye research
Volume26
Issue number5
DOIs
StatePublished - May 1978

Keywords

  • age-related changes
  • electrophoresis
  • lens proteins
  • long-lived proteins
  • polypeptide composition
  • post-synthetic modifications
  • β-crystallin

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems
  • Cellular and Molecular Neuroscience

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