Propriétés physico-chimiques et immunologiques des γG humaines modifiees—II: Hétérogénéité structurale du facteur Gm(1)

Abstract

In the present work, we have studied the modifications brought to the serological expression of the Gm(1) factor, after a progressive denaturation by succinylation of the normal and myeloma human γG. Purified normal γG and five myeloma γG 1, having a Gm(1) phenotype, were treated by quantities of succinic anhydride going from 0 to 20% in relation with the γG. The quantitative expression of the Gm(1) factor was followed, during the different stages of succinylation, by reactions towards five anti-Gm(1) reagents in three clearly defined groups. The inhibition power of the proteins treated by 10% succinic anhydride disappears completely with two of the agglutinating systems (type I), whereas it remains intact with two other systems, even for degrees of succinylation reaching 20% (type III). Finally, a third intermediate group composed with the last Gm(1) can be detected (type II). These factors allow to be put forward the hypothesis of a probable ‘mosaic’ of the Gm(1) factor.