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. 2014 May;48(100):51–62. doi: 10.1016/j.ibmb.2014.02.005

Fig. 6.

Fig. 6

SDS-PAGE of purified protein fractions. The fractions related to each peak (Fig. 4, lower panel) were loaded on SDS-PAGE for the first peak related fractions (a) and the second peak related fractions (b). No differences in relation to the molecular weight were identifiable through under denature condition. M: weight marker (BSA: 66 kDa, Ovalbumin: 45 kDa, Carbonic anhydrase: 29 kDa, Trypsin inhibitor: 20 kDa, Lactalbumin: 14 kDa).