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A glycoprotein exhibiting a relative molecular mass of about 1000 kDa was purified to homogeneity from culture supernatant of arthritogenic bacteria (Erysipelothrix rhusiopathiae, strain T28) by ultrafiltration, ammonium sulfate precipitation, molecular mass exclusion, and ion exchange chromatography. Fractions obtained were analysed for their antigenic content by an enzyme linked immunosorbent assay (ELISA) using rabbit immune serum raised against this strain of Erysipelothrix rhusiopathiae. Distinct monoclonal antibodies obtained from rats suffering from erysipelas polyarthritis display a unique property by inducing very efficiently protective and regulatory mechanisms while being unable to generate classical "passive immunity". These "inductive" monoclonal antibodies recognize most likely linear epitopes on the purified glycoprotein. This makes it a prime source for analysing the target structure of these in vivo "inductive" antibodies.

biological chemistry hoppe-seyler

Isolation of a High-Molecular Mass Glycoprotein from Culture Supernatant of an Arthritogenic Strain of the Bacteria  Erysipelothrix rhusiopathiae  Reacting with “Inductive” Monoclonal Antibodies Derived from Rats with Erysipelas Polyarthritis