• Journal of the Korean Society of Food Science and Nutrition
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• v.23 no.3
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• pp.515-519
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• 1994

The ComparativThe comperisons of Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) which have been studied in our laboratory are summerized. The recoveries of pure lectins are 0.12% and 0.014%, respectively. They seems to have slight differences in isoelectric points(pH) ; 5.19~5.67 for KBL and 6.41~7.42 for TTL. The minimum concentrations of HA are $2.8\mu\textrm{g}/ml\;and\;21.6\mu\textrm{g}/ml$. The enzymatic modification on HA, growth inhibition, inhibition of nutritional absorption and binding capacities (FITC, $^3H$) of KBL are demonstrated to be much greater than those of TTL.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.4
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• pp.494-499
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• 1993

The morphological and histochemical observation of the lectin binding to intestine in vivo or in vitro was investigated. Our finding demonstrates the validity of semi-quantitative estimates of lectin binding to mouse intestine. The fluorescence patterns obtained after treatment of intestine sections with FITC-conjugated lectin revealed that Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) were localized on the cell membrane, especially the top and upper sites of the villi and showed that KBL was more strongly located than TTL under various conditions. In the reverted intestine of mice fed lectin, the villi were considerably disordered and conspicuously disrupted.

• Journal of the Korean Society of Food Science and Nutrition
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• v.22 no.4
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• pp.489-493
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• 1993

The major objective of this study carried out was to compare the binding of Kintoki bean lectin (KBL) and Taro tuber lectin (TTL) to the mouse intestinal segments using $^3$H-labeled lectins and to assess the effect of such binding on the ability of the small intestine. Binding of $^3$H-KBL or $^3$H-TTL was studied under various conditions of time course, temperature, concentration, pH and additives of sugars, EDTA or unlabeled native lectin. The interaction of the lectins to intestinal tissue was stronger in KBL than in TTL, which was supposed to be the major reason for the stronger antinuritional enen of KBL. The optimal binding conditions were at 37$^{\circ}C$ for 60mins and at pH 7. The binding of both lectins were inhibited by fetuin and EDTA.