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Table 6 The difference of SDS-PAGE and 2-DE map of wild rice species and identification of the corresponding protein spots among three wild rice species

From: Proteomic analysis of seed storage proteins in wild rice species of the Oryza genus

Differential protein region

SDS-PAGE

2-DE map

*2-DE map identification by Xie et al.[[12]]

LC/ESI-MS/MS identification of wild rice species

I, Glutelin acidic subunit

Expression of protein from 35 kDa to 34 kDa in this area of O. meyeriana was significantly higher than that of other materials.

The expression of protein spot 14, spot 15 and spot 16 with molecular weight 34 kDa and pI 8.0 to 9.5 obviously increased in O. meyeriana.

Corresponding to spots 15 and 16 in the corresponding region which were identified as the 56 kDa putative glutelin type-B 2 precursor

No

α-1 subunit of glutelin acidic subunit was absent, while a new protein band of about 40 kDa appeared in O. meyeriana.

Specific protein spot 23 (34 kDa, pI 5.95), spot 24 (34 kDa, pI 5.72) and spot 25 (34 kDa, pI 5.54) were observed in O. officinalis; Protein spot 7 (35 kDa, pI 7.22), spot 13 (34 kDa, pI 7.58) and spot 14 (34 kDa, pI 8.11) were absent in O. officinalis;.

Corresponding to spot 14 in the corresponding region which was identified as the 56 kDa putative glutelin type-B 2 precursor.

Protein spot 14: hypothetical protein

 

Two unique protein spots 21 (pI 6.68,34 kDa) and 22 (pI 6.83,34 kDa) were detected in O. rufipogon.

No corresponding spot in the corresponding area.

Protein spot 23: 56 kD glutelin type-A 2 precursor

II, Glutelin precursor

The expression of 57 kDa glutelin precursor increased in O. rufipogon.

The expression of protein in this region with 57 kDa, and pI 9.0-10.0 increased in the three wild rice species

Corresponding to spot 5 in the corresponding region which was identified as 56 kDa glutelin type I precursor.

No

IV, Water-soluble protein

The expression contents of 62 kDa protein in wild rice species were higher than two cultivated rice materials.

Four consecutive protein spots 1, 2, 3 and 4 with 62 kDa and pI from 4.5 to 7.5 were elevated in water-soluble protein area of the three wild rice species.

Corresponding to spots 1, 2, 3 and 4 in the corresponding region which were identified as glycogen (starch) synthase.

No

 

Two unique protein groups were present in O. meyeriana.

No corresponding spot in the corresponding area.

No

V, Globulin

The 26 kDa protein band was absent, and a new 28 kDa protein band appeared in O. meyeriana.

Protein spots 17 (pI 5.44, 24 kDa) and 18 (pI 5.65, 24 kDa) were absent in O. officinalis, meanwhile a protein spot 39 with 24 kDa and pI 6.27 was present.

Corresponding to spots 17 and 18 in the corresponding region which were identified as 21 kDa α globulin, and the experimental protein molecular weight is 26 kDa.

No

The 26 kDa protein band in O. officinalis decreased remarkably.

The expression of protein spot 18 notably higher than the other material in O. meyeriana.

  1. *The study of endosperm protein 2-DE map identification by Xie et al.