Open AccessBinding of avidin to bacteria and to the outer membrane porin of Escherichia coli
Author(s) -
Korpela Jukka,
Salonen EevaMarjatta,
Kuusela Pentti,
Sarvas Matti,
Vaheri Antti
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb00344.x
Subject(s) - avidin , porin , bacterial outer membrane , escherichia coli , bacteria , biotin , biochemistry , binding site , biology , gram negative bacteria , chemistry , microbiology and biotechnology , genetics , gene
The binding of avidin to different bacteria was studied using tetramethylrhodamine isothiocyanate (TRITC)‐conjugated avidin in fluorescence microscopy, enzyme immunoassay and [ 14 C]biotin‐avidin complex. We observed binding of avidin to all Gram‐negative bacteria tested and to some Gram‐positive bacteria. The binding was dose‐dependent, reached the maximum in 10 min, was optimal at physiological pH and occurred at 4°C, 22°C, and 37°C. This binding of avidin was independent of the saturation of its biotin‐binding sites. The avidin receptor of the cell envelope of Escherichia coli K‐12 was shown to be the major porin protein (OmpF/OmpC) of the outer membrane.