Shida K, Takamizawa K, Osawa T
Yakult Central Institute for Microbiological Research, Tokyo, Japan.
Biosci Biotechnol Biochem. 1996 Sep;60(9):1492-4. doi: 10.1271/bbb.60.1492.
The inhibition by lactose-alpha-lactalbumin amino carbonyl product of Escherichia coli heat-labile enterotoxin was studied by GM1-ELISA and by assay with CHO-K1 cells. The product dose-dependently inhibited the binding of the enterotoxin to GM1 ganglioside and decreased the morphological change of CHO-K1 cells caused by this toxin. The results suggest that this product may be a receptor analogue in the intestine.
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