Biochemistry of Bovine Lens Proteins. III. Chemical and Physical Properties of α-Crystallin Subunits

Winifred G. Palmer, John Papaconstantinou

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

The α-crystallins of the adult bovine lens can be resolved into five components by DEAE-cellulose chromatography. These fractions have similar physicochemical properties and are immunochemically identical. They can be progressively disaggregated into their component subunits by increasing concentrations of sodium dodecyl sulfate (SDS). All five α-crystallins respond identically with this SDS treatment. Chromatography of 7 M urea treated α-crystallins on 7 M urea equilibrated DEAE-cellulose revealed that the five α- crystallins are composed of the same subunits, accounting for their immunochemical identity. However, the quantity of the different subunits in each α-crystallin varies, thus accounting for the differences in their chromatographic properties. Differences between the isolated subunits have been revealed by peptide mapping.

Original languageEnglish (US)
Pages (from-to)243-253
Number of pages11
JournalBiochemistry
Volume7
Issue number1
DOIs
StatePublished - Jan 1 1968
Externally publishedYes

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Crystallins
Biochemistry
Chemical properties
Physical properties
DEAE-Cellulose
Chromatography
Sodium Dodecyl Sulfate
Urea
DEAE-Cellulose Chromatography
Peptide Mapping
Lenses
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

Biochemistry of Bovine Lens Proteins. III. Chemical and Physical Properties of α-Crystallin Subunits. / Palmer, Winifred G.; Papaconstantinou, John.

In: Biochemistry, Vol. 7, No. 1, 01.01.1968, p. 243-253.

Research output: Contribution to journalArticle

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