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. 2008 Sep;148(1):620–641. doi: 10.1104/pp.108.123141

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
a

Protein numbering following Arabidopsis seed protein reference maps available at http://www.seed-proteome.com.

b

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.

c

Listed proteins correspond to previously identified proteins (Gallardo et al., 2001, 2002a; Rajjou et al., 2004, 2006a; Job et al., 2005).