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

J. Samuel Zigler

Research output: Contribution to journalArticle

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 - 1978
Externally publishedYes

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Crystallins
Lenses
Peptides

Keywords

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

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Age-related changes in the polypeptide composition of β-crystallin from bovine lens. / Zigler, J. Samuel.

In: Experimental Eye Research, Vol. 26, No. 5, 1978, p. 537-546.

Research output: Contribution to journalArticle

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