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伴刀豆球蛋白A诱导的耐格里属原虫凝集

Concanavalin A-induced agglutination of Naegleria.

作者信息

Josephson S L, Weik R R, John D T

出版信息

Am J Trop Med Hyg. 1977 Sep;26(5 Pt 1):856-8. doi: 10.4269/ajtmh.1977.26.856.

Abstract

Concanavalin A (Con A) agglutinated all Naegleria gruberi strains tested but did not agglutinate any N. fowleri strains tested. Agglutination was time and temperature dependent and Con A concentration and ameba concentration dependent over certain ranges. Agglutination increased to maximum up to 1 h incubation with Con A. At least 1 X 10(6) amebae/ml were needed for maximum agglutination, and Con A concentrations higher than 100 microgram/ml did not appreciably increase agglutination. Incubation of 4 degrees C or with 10 mM alpha-methyl-D-mannoside inhibited agglutination of N. gruberi. These data indicate a difference in polysaccharide structure of cell membranes of N. fowleri and N. gruberi.

摘要

刀豆球蛋白A(Con A)能凝集所有测试的格氏耐格里阿米巴菌株,但不能凝集任何测试的福氏耐格里阿米巴菌株。凝集作用具有时间和温度依赖性,并且在一定范围内还依赖于Con A浓度和阿米巴浓度。与Con A孵育长达1小时,凝集作用增强至最大值。最大凝集作用需要至少1×10⁶个阿米巴/毫升,并且Con A浓度高于100微克/毫升时,凝集作用不会显著增加。4℃孵育或与10 mMα-甲基-D-甘露糖苷孵育可抑制格氏耐格里阿米巴的凝集。这些数据表明福氏耐格里阿米巴和格氏耐格里阿米巴细胞膜多糖结构存在差异。

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