Disulphide Bridges of Immunoglobin G1 Heavy Chains

Abstract

THE immunoglobulins G1 represent the major component of human immunoglobulins, with a basic four chain structure consisting of two heavy and two light chains joined by disulphide bridges1. (The nomenclature used is based on that recommended by the World Health Organization (1966).) The light chains are made up of two sections—an invariable C-terminal section characteristic of each type, and a variable N-terminal section specific to each clone2–4. Peptide maps of Fd fragments5,6 suggest that a similar situation holds in heavy chains. In light chains the two sections are folded, each by a single disulphide bridge, to give two loops of almost equal size—the invariable C-terminal loop and the variable N-terminal loop7. The Fc region of human G immunoglobulins includes two intrachain disulphide bridges which impose on it a ring structure, again made up of an N-terminal and a C-terminal loop, resembling the ring structure of light chains8. In this communication, we present evidence which suggests further similarities between disulphide bridges of light and heavy chains. We also present results concerning a peptide containing both the heavy-light and heavy-heavy interchain disulphide bridges.

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FRANGIONE, B., MILSTEIN, C. Disulphide Bridges of Immunoglobin G1 Heavy Chains. Nature 216, 939–941 (1967). https://doi.org/10.1038/216939b0

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