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. 2018 Jan 15;55(4):1256–1269. doi: 10.1007/s13197-018-3036-y

Fig. 1.

Fig. 1

Fig. 1

Fig. 1

a SDS-PAGE analysis of gliadins of different durum wheat accessions. Gliadins were extracted from meal of durum wheat by 60% ethanol and subjected to SDS-PAGE analysis under non-reducing conditions by omitting β-mercaptoethanol from sample buffer. After electrophoresis, gels were fixed in 8% tri chloro acetic acid for 30 min at room temperature and 20 ml of 0.2% (w/v) coomassie brilliant blue R 250 dye, dissolved in absolute ethanol and passed through Whatman filter paper no. 1, was mixed in fixing solution. Gels were washed thoroughly with de-ionized water and scanned with HP G4010 flatbed scanner. The molecular weight analysis was done by using AlphaEase® FC v 6.0.0 gel analyzer software. b SDS-PAGE analysis of gliadins of different durum wheat accessions. The extraction and processing of gliadins was done as described in a. c Comparative SDS-PAGE analysis of gliadins between durum wheat and standard wheat. MACS9, PDW233, HI8498 were used as standards for which the gliadin architecture was well established. d SDS-PAGE analysis of different glutenins-subunits extracted from different durum wheat accessions. Reduced and alkylated glutenins were extracted from fine flour of durum wheat by glutenin extraction buffer (80 mM Tris HCl, pH 8.0, 50% propanol, 1% DL-Dithiothreitol, 0.4% 4-vinyle pyridine) thrice at 65 °C for 30 min each and subjected to SDS-PAGE analysis under reducing conditions. After electrophoresis, gels were stained in a staining solution containing 0.2% (w/v) commassie brilliant blue R 250 dye in 50% methanol for overnight and gels were destained in 50% methanol and washed thoroughly with de-ionized water. De-stained gels were scanned with HP G4010 flatbed scanner and the molecular weight analysis was done by using AlphaEase FC v 6.0.0 gel analyzer software. e SDS-PAGE analysis of different glutenins of different durum wheat accessions. Extraction, electrophoresis and gel documentation of durum glutenin were done as described in a. Molecular of different polypeptides are in kilo Dalton (kDa). HMW-GS molecular weights a = 113 kDa; b = 110 kDa; c = 107 kDa; d = 101 kDa; e = 97 kDa; f = 95 kDa; g = 92 kDa; h = 91; i = 88 kDa; j = 83 kDa; k = 81 kDa