Inhibition of Escherichia coli heat-labile enterotoxin by an amino carbonyl product, lactose-alpha-lactalbumin.
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.
Shida
K
K
Yakult Central Institute for Microbiological Research, Tokyo, Japan.
Takamizawa
K
K
Osawa
T
T
D000818:Animals; D001427:Bacterial Toxins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D016466:CHO Cells; D006224:Cricetinae; D004768:Enterotoxins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D006031:Glycosylation; D007768:Lactalbumin / Q000737:chemistry*; D007785:Lactose / Q000737:chemistry*; D011956:Receptors, Cell Surface / Q000378:metabolism*
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D011956:Receptors, Cell Surface; C034993:ganglioside receptor; D007768:Lactalbumin; C027538:heat-labile enterotoxin, E coli; D007785:Lactose