SPECIFIC INTERACTION BETWEEN LISTERIA-MONOCYTOGENES AND GLYCOSYLATED ALBUMINS

被引：2
作者：
COTTIN, J
ROBERT, R
DELAJARRIGE, PL
LOISEAU, O
MAHAZA, C
CARBONNELLE, B
SENET, JM
机构：
[1] UFR MED PHARM, PARASITOL LAB, ANGERS, FRANCE
[2] CTR REG LUTTE CANC, ANGERS, FRANCE
[3] CTR HOSP REG & UNIV, BACTERIOL LAB, ANGERS, FRANCE
[4] UFR MED PHARM, IMMUNOL LAB, ANGERS, FRANCE
来源：
RESEARCH IN MICROBIOLOGY | 1991年 / 142卷 / 05期
关键词：
LISTERIA-MONOCYTOGENES; LECTIN; ADHESIN; GLYCOSYLATED ALBUMINS; BINDING CHARACTERISTICS;
D O I：
10.1016/0923-2508(91)90183-B
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
We have previously shown that Listeria monocytogenes serovar 1/2b can bind strongly to bovine albumin (BA) glycosylated by glucosamine or fucosylamine with about 20 to 30 carbohydrate residues per albumin molecule. We now show that the binding is time-dependent, reversible, saturable and specific. The two glycosylated compounds inhibit each other competitively. Scatchard analysis showed that about 100 molecules of BA-glucosamide (heptameric configuration) and 14,300 molecules of BA-fucosylamide (monomeric configuration) bound per bacterial cell. The apparent dissociation constants for BA-glucosamide and BA-fucosylamide were found to be 3.9 x 10(-14) M and 3.5 x 10(-13) M, respectively.
引用
收藏
页码：499 / 507
页数：9
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