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Original Articles

Comparative study on the stability of soybean (Glycine max) β-conglycinin in vivo

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Pages 295-304 | Received 29 Apr 2009, Published online: 13 Nov 2009

Figures & data

Table 1. Composition of the diets, as-fed basis (%).

Figure 1.  SDS-PAGE of β-conglycinin. The protein molecular weight marker (low; KDa): phosphorylase b 97.200; bovine serum albumin, 66.400; ovalbumin, 44.300; carbonic anhydrase, 29.000; soybean inhibitor, 201.00; α-lactalbumin, 14.300.

Figure 1.  SDS-PAGE of β-conglycinin. The protein molecular weight marker (low; KDa): phosphorylase b 97.200; bovine serum albumin, 66.400; ovalbumin, 44.300; carbonic anhydrase, 29.000; soybean inhibitor, 201.00; α-lactalbumin, 14.300.

Table 2. Analysis of the immunoreactivity disappearance proportion for β-conglycinin in digesta.

Figure 2.  SDS-PAGE gels of β-conglycinin in the digesta. Lane 1: the protein molecular weight marker (low; KDa): phosphorylase b 97.200; bovine serum albumin, 66.400; ovalbumin, 44.300; carbonic anhydrase, 29.000; soybean inhibitor, 201.00; α-lactalbumin, 14.300. Lane 2: purified β-conglycinin (added to diets). Lane 3–7: β-conglycinin extracted from the digesta of stomach, upper-jejunum, middle-jejunum, ileum and caecum.

Figure 2.  SDS-PAGE gels of β-conglycinin in the digesta. Lane 1: the protein molecular weight marker (low; KDa): phosphorylase b 97.200; bovine serum albumin, 66.400; ovalbumin, 44.300; carbonic anhydrase, 29.000; soybean inhibitor, 201.00; α-lactalbumin, 14.300. Lane 2: purified β-conglycinin (added to diets). Lane 3–7: β-conglycinin extracted from the digesta of stomach, upper-jejunum, middle-jejunum, ileum and caecum.

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