Identification and partial purification of K88ab Escherichia coli receptor proteins in porcine brush border membranes.
Six receptor proteins, with molecular masses ranging from 94 to 27 kDa, that bind to Escherichia coli K88ab fimbriae were recovered from brush border membranes and were detected after solubilization with Triton X-114. The recovery of these receptor proteins in the aqueous phase suggests their peripheral localization. The 63-, 60- and 33-kDa K88ab binding proteins were recovered using gel-filtration chromatography of the aqueous phase.
Caloca
M J
MJ
Departamento de Bioquímica y Biología Molecular, Universidad de León, Spain.
Suárez
S
S
Soler
J
J
D000818:Animals; D000942:Antigens, Bacterial / Q000302:isolation & purification* / Q000378:metabolism; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000254:growth & development*; D029968:Escherichia coli Proteins / Q000302:isolation & purification* / Q000378:metabolism; D036781:Fimbriae Proteins / Q000302:isolation & purification* / Q000378:metabolism; D008871:Microvilli / Q000382:microbiology*; D013552:Swine
D000942:Antigens, Bacterial; D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; C026888:K88 antigen, E coli; D036781:Fimbriae Proteins