{"title":"凝集素与微生物的非特异性和协同结合。","authors":"L D Kahn","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Binding of lectins to microbial cell walls was investigated by fluorimetric titration and Scatchard plot. Data were correlated with agglutinability. Concanavalin A and lectins of wheat germ, soybean, pea, lentil, and peanut were tested against Escherichia coli. Micrococcus luteus, Lactobacillus plantarum, and Bacillus subtilis. In cases where binding occurred, it was either nonspecific or positively cooperative. Agglutination was observed only in those combinations of lectin and microorganism that showed positive cooperative binding, suggesting a definite relation between binding and agglutination. Lectins binding to the same carbohydrate did not necessarily bind to the same microorganism, confirming the complexity of the lectin-receptor bond.</p>","PeriodicalId":20124,"journal":{"name":"Physiological chemistry and physics","volume":"14 1","pages":"3-7"},"PeriodicalIF":0.0000,"publicationDate":"1982-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Nonspecific and cooperative binding of lectins to microorganisms.\",\"authors\":\"L D Kahn\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Binding of lectins to microbial cell walls was investigated by fluorimetric titration and Scatchard plot. Data were correlated with agglutinability. Concanavalin A and lectins of wheat germ, soybean, pea, lentil, and peanut were tested against Escherichia coli. Micrococcus luteus, Lactobacillus plantarum, and Bacillus subtilis. In cases where binding occurred, it was either nonspecific or positively cooperative. Agglutination was observed only in those combinations of lectin and microorganism that showed positive cooperative binding, suggesting a definite relation between binding and agglutination. Lectins binding to the same carbohydrate did not necessarily bind to the same microorganism, confirming the complexity of the lectin-receptor bond.</p>\",\"PeriodicalId\":20124,\"journal\":{\"name\":\"Physiological chemistry and physics\",\"volume\":\"14 1\",\"pages\":\"3-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1982-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Physiological chemistry and physics\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Physiological chemistry and physics","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Nonspecific and cooperative binding of lectins to microorganisms.
Binding of lectins to microbial cell walls was investigated by fluorimetric titration and Scatchard plot. Data were correlated with agglutinability. Concanavalin A and lectins of wheat germ, soybean, pea, lentil, and peanut were tested against Escherichia coli. Micrococcus luteus, Lactobacillus plantarum, and Bacillus subtilis. In cases where binding occurred, it was either nonspecific or positively cooperative. Agglutination was observed only in those combinations of lectin and microorganism that showed positive cooperative binding, suggesting a definite relation between binding and agglutination. Lectins binding to the same carbohydrate did not necessarily bind to the same microorganism, confirming the complexity of the lectin-receptor bond.