Isolation of Human Reagins Differing in Their Affinity for Ragweed Immunosorbent

Abstract

Reaginic antibodies to ragweed pollen which had been adsorbed to cellulose-allergen immunosorbents were eluted in the presence of homologous or heterologous serum protein(s) at a concentration of 3–7 mg/ml with gly-HCl at pH 2.5, or 6 m urea at pH 7.4. These extraneous serum proteins exerted a stabilizing effect on the eluted reagins. Two groups of reagins differing in their affinity for the allergen(s) were sequentially eluted from the immunosorbent with gly-HCl and Nal regardless of the order of addition of these eluting agents. Moreover, specific elution of some reagins was achieved with a low molecular weight, hapten-like preparation of ragweed pollen.

The use of antifibrin antibodies for the destruction of tumor cells

“…It has been shown in another study in this laboratory (Kisil et al, 1974) that denaturation of antibodies occurs at low concentration, and particularly readily at the low pH used for their elution from the immunosorbent; this may be minimized by adding proteins such as serum albumin to act as stabilizers. It has been shown in another study in this laboratory (Kisil et al, 1974) that denaturation of antibodies occurs at low concentration, and particularly readily at the low pH used for their elution from the immunosorbent; this may be minimized by adding proteins such as serum albumin to act as stabilizers.…”