| Abstract: | The formation of D -penicillamine-L -cysteine mixed disulfide from benzylpenicilloic acid, benzylpenilloic acid and benzylpenicilloyl amide derivatives in L -cysteine suspensions at pH 7,6 and 37° was studied. The reaction is faster than direct penicilloylation of proteins known to be a route to penicilloyl antigenic determinants. The production of S-bound penicillamine on protein from penicilloyl compounds must therefore definitely be considered as a potential antigenforming step. The reaction may be partly if not fully blocked by acylation of the thiazolidine nitrogen of penicilloyl compounds. When formylation is applied a considerable reduction of the capacity of penicilloyl antigenic determinants to interact with anti-penicilloyl antibody is noted. A D -penicillamine-specific test antigen was prepared by binding D -penicillamine via thioether links to a partly succinylated poly-L -lysine. Clinical test reactions elicited with this conjugate and with penicilloic acid cannot be well correlated. Penicilloic acid probably detects reactions of undefined specificity in addition to D -penicillamine-specific ones. |
