STOICHIOMETRY OF MALTODEXTRIN-BINDING SITES IN LAMB, AN OUTER-MEMBRANE PROTEIN FROM ESCHERICHIA-COLI

被引：13

作者：

GEHRING, K ^{[1
]}

CHENG, CH ^{[1
]}

NIKAIDO, H ^{[1
]}

JAP, BK ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY LAWRENCE BERKELEY LAB,DEPT MOLEC & CELL BIOL,BERKELEY,CA 94720

来源：

JOURNAL OF BACTERIOLOGY | 1991年 / 173卷 / 06期

关键词：

D O I：

10.1128/jb.173.6.1873-1878.1991

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

We have directly measured the stoichiometry of maltodextrin-binding sites in LamB. Scatchard plots and computer fitting of flow dialysis (rate-of-dialysis) experiments clearly establish three independent binding sites per LamB trimer, with a dissociation constant of approximately 60-mu-M for maltoheptaose. The current model for LamB's function as a specific pore is discussed with respect to the symmetry in LamB's kinetic properties and the implications of our results.

引用

页码：1873 / 1878

页数：6

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