Table II.
Arabidopsis proteins whose abundance significantly decreased in dry mature seeds according to controlled deterioration time
No.a | Experimental Molecular Mass | Experimental pI | Arabidopsis Protein Name | Theoretical Molecular Mass | Theoretical pI | AGI No. | Coverage | Relative Abundanceb | T1/2 |
---|---|---|---|---|---|---|---|---|---|
kD | kD | ratio 7 d:0 d | d | ||||||
4c | 57.35 | 4.89 | Tubulin β2β3 chain | 50.73 | 4.7 | At5g62700 | 35% | 0.26 ± 0.01 | 0.17 ± 0.05 |
146c | 37.67 | 5.03 | MST | 41.89 | 5.95 | At1g79230 | 35% | 0.33 ± 0.05 | 1.12 ± 0.33 |
254c | 22.1 | 4.96 | Dehydrin | 18.44 | 7.95 | At5g66400 | 6% | 0.13 ± 0.04 | 0.93 ± 0.15 |
255c | 21.65 | 5.18 | Dehydrin | 18.44 | 7.95 | At5g66400 | 6% | <0.22 | >7 |
304c | 69.3 | 5.56 | Phosphoglucomutase | 63.44 | 5.73 | At1g70730 | 37% | 0.30 ± 0.04 | 0.37 ± 0.12 |
311c | 14.1 | 3.2 | β-Cruciferin 12S (seed storage protein fragment) | 21.20 | 6.19 | At4g28520 | 11% | 0.19 ± 0.01 | 0.56 ± 0.04 |
Protein numbering following Arabidopsis seed protein reference maps available at http://www.seed-proteome.com.
Data obtained from densitometric analysis of individual spots from proteins on 2D gels stained with silver nitrate (see Fig. 2A for an example of a 2D gel): normalized spot volume in the deteriorated seeds (7 d of CDT) divided by the normalized spot volume in the nondeteriorated control seeds (0 d of CDT), from five different gels and three independent extractions.
Listed proteins correspond to previously identified proteins (Gallardo et al., 2001, 2002a; Rajjou et al., 2004, 2006a; Job et al., 2005).