Table IX.

Arabidopsis polypeptides whose abundance specifically varied during priming

Protein Type	No.	Exp. Mr	Exp. pI	Arabidopsis Protein Name	Cov.	Theo. Mr	Theo. pI	Accession No.	Rel Abund HPa	Rel Abund OPa
					%
7	4	57.35	4.89	β-2 Tubulin	36	50.73	4.70	166898	4.2 ± 0.3	4.1 ± 0.4
7	89	15.80	5.72	β-Subunit of 12S-2 seed storage proteinb	36	20.80	7.03	P15456	4.0 ± 0.1	2.6 ± 0.2
7	12	16.14	5.71	β-Subunit of 12S-2 seed storage proteinc	30	20.80	7.03	P15456	3.4 ± 0.1	2.0 ± 0.1
9	8	17.93	4.99	Class I heat shock protein 17.4	26	17.45	5.20	P19036	1.1 ± 0.1	4.5 ± 0.5
9	9	17.94	5.50	Heat shock protein 17.7	42	17.77	5.36	S71248	1.3 ± 0.1	4.5 ± 0.2
10	1	79.36	5.08	Luminal-binding protein	20	71.17	5.08	1695719	0.9 ± 0.1	0.3 ± 0.03
11	17	73.40	6.58	Phosphoenolpyruvate carboxykinase	17	73.40	6.61	7449802	4.0 ± 0.2	1.0 ± 0.1
11	23	56.48	6.64	Catalase 2	34	56.91	6.63	P25819	3.4 ± 0.1	1.3 ± 0.1
11	6	54.71	5.06	Tubulin α-Chain	58	49.54	4.93	320183	2.7 ± 0.2	0.9 ± 0.1

Type-7 proteins, proteins whose level specifically increased during both hydropriming (HP) and osmopriming (OP); type-9 and type-10 proteins, proteins whose level specifically increased or decreased during osmopriming, respectively; type-11 proteins, proteins whose level specifically increased during hydropriming. Cov., Coverage; Exp., experimental; Rel Abund, relative abundance; Theo., theoretical.

^a Data obtained from densitometric analysis of individual spots (see Fig. 2): normalized spot volume in the primed seeds divided by the normalized spot volume in the dry mature seeds ± sd. 

^b Theoretical M_r and pI values matched the experimental values by removing 15 amino acids from the C-terminal sequences. 

^c Theoretical M_r and pI values matched the experimental values by removing 14 amino acids from the C-terminal sequences.