Table I.
Arabidopsis proteins whose abundance was significantly different in dry mature Ler seeds than in dry mature seeds from the tt2-1 mutant
| No.a | Exp. MM | Exp. PI | Arabidopsis Protein Nameb | Cov. | Theo. MM | Theo. PI | AGI No. | Relative Abundancec |
|---|---|---|---|---|---|---|---|---|
| kD | % | kD | ||||||
| 17 | 72.98 | 6.57 | Phosphoenolpyruvate carboxykinase | 17 | 73.40 | 6.61 | At4g37870 | 1.6 ± 0.06 |
| 25 | 23.32 | 6.89 | β-Cruciferin 12S seed storage protein | 43 | 21.20 | 6.19 | At4g28520 | 3.8 ± 0.05 |
| 69 | 43.67 | 6.29 | 12S Cruciferin precursor | 18 | 50.56 | 6.53 | At1g03880 | 2.0 ± 0.08 |
| 160 | 82.27 | 5.94 | Met synthase | 12 | 84.36 | 6.09 | At5g17920 | 3.0 ± 0.06 |
Cov., coverage; Exp., experimental; Theo., theoretical.
Protein numbering following Gallardo et al. (2001, 2002a) and Arabidopsis seed protein reference maps (http://seed.proteome.free.fr).
Listed proteins correspond to previously identified proteins (Gallardo et al., 2001, 2002a).
Data obtained from densitometric analysis of individual spots from 2D gels colored with silver nitrate (see Fig. 5 for an example of 2D gel): normalized spot volume in the mature dry tt2-1 mutant seeds divided by the normalized spot volume in the wild-type Ler dry mature seeds ±sd, from three different gels and independent extractions.