Date of Award

Spring 1974

Document Type

Thesis

Department

Life & Environmental Sciences

First Advisor

Rev. James Sullivan

Second Advisor

John Christenson

Third Advisor

Rev. Joseph Harrington

Abstract

The simplest subunit by which the immune systems of higher animals function is the immunoglobulin. Immunoglobulins are proteins endowed with antibody activity, that is, the ability to bind and inactivate those foreign substances capable of illiciting an antigenic response. Antigenic types and classes of immunoglobulins are established. The Bence- Jones dimer, by its very nature, has significance as a model for antibody structure and function. The lambda-type chain appears to have a striking similarity with the IgG light chains. The models of the Bence-Jones dimer that have been constructed at Argonne National Laboratory were sealed by x-ray crystallography which suggest the antigenic specificity of the two light chains of the IgG immunoglobulin.

The blocked N-terminal of the Bence-Jones protein has been unblocked with the ensyme, Pyrrolidonecarboxylyl Peptidase, The scheme for the isolation of this enzyme is contained within this text, Pyrrolidonecarboxylyl Peptidase was isolated from Pseudomonas fluorescens has proved to be specific for the peptide linkage of PGA-Ser on the N-terminal of the Bence-Jones Dimer, Ninety per cent cleavage of the peptide bond was obtained, which is signigicant enough for crystallographic study of the N-terminal.

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