Fragmentation of human IgG by a new protease isolated from the basidiomycete Armillaria mellea.
- 1 November 1975
- journal article
- Vol. 29 (5) , 921-31
Abstract
Digestion of human IgG by a new lysine-specific protease, isolated from the basidiomycete Armillaria mellea, produced Fc and Fab fragments similar to those produced by papain digestion of the same molecule. Digestion appeared to be restricted to a single cleavage point within the hinge region of the IgG molecule. Myeloma proteins of IgG1, IgG3 and IgG4 subclasses were found to be digested at an extremely rapid rate whereas IgG2 myeloma proteins appeared to be resistant to digestion by this enzyme.This publication has 8 references indexed in Scilit:
- The use of baboon IgG-sensitized sheep erythrocytes as an alternative indicator system in the study of the interaction of rheumatoid factor with human IgGImmunochemistry, 1975
- Biological activities associated with the Facb fragment of rabbit IgGImmunochemistry, 1973
- THE COVALENT STRUCTURE OF AN ENTIRE γG IMMUNOGLOBULIN MOLECULEProceedings of the National Academy of Sciences, 1969
- Subfragments from the Fc fragment of human immunoglobulin G. Isolation and physicochemical characterizationBiochemical Journal, 1968
- BIOLOGICALLY ACTIVE WATER-INSOLUBLE PROTEIN POLYMERS .I. THEIR USE FOR ISOLATION OF ANTIGENS AND ANTIBODIES1967
- REACTIVITY OF RHEUMATOID FACTOR WITH RABBIT GAMMA-GLOBULIN1965
- Reaction of Rheumatoid Sera with Fragments of Papain-Digested Rabbit Gamma Globulin.Experimental Biology and Medicine, 1961
- STRUCTURAL UNITS OF HUMAN 7S GAMMA GLOBULIN *Journal of Clinical Investigation, 1960