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 language | English (US) |
|---|---|
| Pages (from-to) | 243-253 |
| Number of pages | 11 |
| Journal | Biochemistry |
| Volume | 7 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 1 1968 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry