| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871311 | FEBS Letters | 2012 | 4 Pages |
Abstract
⺠Trxh reduces all five disulfide bonds in barley LDI causing inactivation. ⺠LDI is protected against Trxh reduction when complexed to LD. ⺠Trxh shows preference for the glutathionylated cysteine disulfide in LDI. ⺠Deglutathionylation appears not to be connected with inactivation of LDI. ⺠Conformational destabilisation of LDI is proposed to cause inactivation.
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Authors
Johanne Mørch Jensen, Per Hägglund, Hans Erik Mølager Christensen, Birte Svensson,