STUDIES ON ANTIGENICITY
Open Access
- 1 November 1964
- journal article
- research article
- Published by Rockefeller University Press in The Journal of Experimental Medicine
- Vol. 120 (5) , 955-965
- https://doi.org/10.1084/jem.120.5.955
Abstract
The enzymatic degradation of fluorescein conjugates of poly-L-lysine, poly-D-lysine, and exhaustively succinylated poly-L-lysine by aqueous extracts of spleens from "responder" (guinea pigs which can develop immune responses to hapten-poly-L-lysine conjugates) and "non-responder" guinea pigs was investigated. The in vivo degradation of H3-tagged dinitrophenyl conjugates of these synthetic polyamino acids was also studied by measuring urinary excretion of radioactive low molecular weight degradation products of these conjugates after their intraperitoneal injection. It was found that both responder and non-responder guinea pigs can degrade succinylated and unsuccinylated poly-L-lysine conjugates into small molecular fragments, but they cannot degrade hapten-poly-D-lysine conjugates. These studies demonstrate that in addition to the known requirements for antigenicity of macromolecules, i.e. the presence of antigenic determinants, and their capacity to be degraded by immunological tissues, the resulting degradation products must undergo certain additional, as yet unidentified, specific metabolic steps in order to induce an immune response.Keywords
This publication has 9 references indexed in Scilit:
- Antigenicity of Hapten Conjugates of Poly-D-lysine and of Poly-L-lysine in Strain 2 Guinea PigsNature, 1964
- STUDIES ON ARTIFICIAL ANTIGENSThe Journal of Experimental Medicine, 1963
- STUDIES ON ARTIFICIAL ANTIGENSThe Journal of Experimental Medicine, 1963
- Basis for the Antigenicity of Hapten-Poly-L-Lysine Conjugates in Random-Bred Guinea PigsNature, 1963
- Antigenicity of Polypeptides (Poly Alpha Amino Acids). X. Studies with Polymers of D Amino Acids.Experimental Biology and Medicine, 1963
- STUDIES ON ARTIFICIAL ANTIGENSThe Journal of Experimental Medicine, 1963
- The isolation and properties of a proteolytic enzyme, cathepsin D, from bovine spleenBiochemical Journal, 1960
- An improved procedure for starch-gel electrophoresis: further variations in the serum proteins of normal individualsBiochemical Journal, 1959
- Editorial: Some Speculations on the Significance of Formation and Persistence of Antigen Fragments in Tissues of Immunized AnimalsBlood, 1957