Nakata S, Kimura T
J Nutr. 1985 Dec;115(12):1621-9. doi: 10.1093/jn/115.12.1621.
The present study was undertaken to provide further evidence for the mechanisms proposed for the toxicity of ingested bean lectins in animals: to show the stability of concanavalin A (Con A) in the gastrointestinal tract so that it has enough time to interact with some enzymes localized in the intestinal membrane and to find its effect on the activities of those enzymes that have been adopted as criteria for adaptive changes in response to altered diets, namely intestinal sucrase, alkaline phosphatase and leucine aminopeptidase. Significant amounts of ingested Con A were recovered unaltered (as seen from affinity chromatography and electrophoresis) from the cecal content of rats 4 h after its oral administration and from feces (90% recovery) 4 d later. This indicated that Con A is quite stable during its passage through the gastrointestinal tract. Con A, given at a level of 0.3 or 0.5% in the diet, completely prevented adaptive changes in the activities of those enzymes. These results substantiate the mechanisms proposed earlier by other investigators that the toxicity of ingested bean lectins involves their binding to the luminal surface of the small intestine, where they disturb the function of the brush border membrane.
证明伴刀豆球蛋白A(Con A)在胃肠道中的稳定性,使其有足够时间与位于肠膜的某些酶相互作用,并研究其对那些被用作适应饮食变化的适应性改变指标的酶活性的影响,即肠蔗糖酶、碱性磷酸酶和亮氨酸氨肽酶。口服Con A 4小时后,在大鼠盲肠内容物中以及4天后在粪便中(回收率90%)发现大量未改变的摄入Con A(从亲和色谱和电泳结果可见)。这表明Con A在通过胃肠道的过程中相当稳定。饮食中Con A含量为0.3%或0.5%时,完全阻止了这些酶活性的适应性变化。这些结果证实了其他研究者先前提出的机制,即摄入的豆类凝集素的毒性涉及其与小肠腔表面的结合,在那里它们会干扰刷状缘膜的功能。