Human reagins to grass pollens and moulds: their purification and physico-chemical characterization.

  • 1 January 1960
    • journal article
    • Vol. 3  (1) , 45-73
Abstract
Chromatography of reaginic sera (to grass pollens and to moulds) on DEAE-cellulose leads to the concentration of reagins in three well separated fractions. They emerge (a) together with siderophilin, (b) with the early albumin-containing fractions, and (c) in association with strongly adsorbed proteins that require a comparatively high ionic strength buffer for their elution. The proportion of reagins in each of these fractions varies with different sera and with small alterations in the experimental procedure. All three reaginic fractions contain small amounts of γ globulins (referred to as R globulins) of mobilities slightly less than that of siderophilin; (c) contains much α2M globulin and there are traces of α2M in (a) and (b). Yet the bulk of the γ globulins are shown to be free from reaginic activity, and the same is true of the α2M and the β2M globulins, of siderophilin and of albumin. The purer the reaginic fractions are the smaller is the portion of the reagins that can be precipitated with the γ globulins by half saturation with ammonium sulphate. In contrast to the bulk of the γ globulins, R globulins and reagins appear to associate readily with other serum proteins, particularly with α2M globulins. Fractionation with sodium sulphate produces three fractions of similar potency although they have little in common; one consists of the bulk of the γ globulins (0–15 per cent w/v), the most active fraction of the remaining globulins (15–18 per cent) and the third fraction (supernatant from the 18 per cent precipitate) of albumin containing some α globulins, but only a trace of γ globulin.