Abstract
A high Mr subunit of wheat glutenin (1Dx2·2*), having an unusually high Mr (approximately 110000), was purified using a combination of preparative isoelectric focusing and reversed-phase high performance liquid chromatography. Comparison of its N-terminal sequence and amino acid composition with those of the allelic subunit 1Dx2 indicate that its greater Mr could be due to the presence of a larger central repetitive domain. Spectrofluorimetric and circular dichroism analyses suggest that an increase in the length of this domain does not affect the conformational properties of the subunit.
| Original language | English |
|---|---|
| Pages (from-to) | 55-60 |
| Number of pages | 6 |
| Journal | Journal of Cereal Science |
| Volume | 23 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 1996 |
| Externally published | Yes |
Keywords
- High M glutenin subunits