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. 2014 Jan 31;26(1):410–425. doi: 10.1105/tpc.113.121376

Figure 1.

Figure 1.

Phenotypic Analyses of the gpa3 Mutant.

(A) Grain-filling process in the wild type and the gpa3 mutant. Values are means ± sd (n = 3).

(B) Transverse sections of representative wild-type and gpa3 mutant dry seeds. Bars = 1 mm.

(C) Scanning electron microscopy images of transverse sections of wild-type and gpa3 mutant grains. Bars = 10 μm.

(D) SDS-PAGE storage protein profiles of dry seeds from the wild type and the gpa3 mutant. pGT, proglutelins; αGT, glutelin acidic subunits; αGlb, α-globulin; βGT, glutelin basic subunits; Pro, prolamins.

(E) Immunoblot analysis of storage proteins from dry seeds of the wild type and the gpa3 mutant, using antiglutelin and anti-α-globulin specific antibodies. Possible partial degradation products of glutelins and α-globulins are labeled with asterisks.

(F) Immunoblot analysis of the glutelin subfamily proteins (GluA, GluB, and GluC) and the molecular chaperones BiP1 and PDI1-1.

Arrows denote the 57-kD proglutelins, while arrowheads indicate the glutelin acidic subunits (black) and basic subunits (red). Antitubulin antibodies were used as a loading control in (E) and (F).