 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](fw5415fig1mag.jpg)
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Figure 1
Purification of the soybean proteins. (a) Purification of the soybean glycinins using a HiPrep 26/60 Sephacryl S-300 HR gel-filtration column at a flow rate of 1 ml min−1. Each collected fraction contained 6 ml of the elution sample. (b) SDS–PAGE analysis under reducing conditions using 11%(w/v) gel and 1 µl of the elution samples at around 110–170 min. Arrows indicate the expected chains of soybean glycinin: A5, A4, A1b (acidic), B2 and B3 (basic) with molecular masses of 10.6, 30.1, 32.1, 20.5 and 20.7 kDa, respectively. X and Y indicate the fractions used for further N-terminal amino-acid sequence analysis of each protein band. |
![[Figure 1]](fw5415fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
