Macroglobulinemia

Korngold, Leonhard; Leeuwen, Gerda Van

doi:10.1084/jem.110.1.1

Cited by 20 publications

(1 citation statement)

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“…Previous data have shown that mild reduction of IgM globulins resulted in the loss of some antigenic determinants (33,34). The results reported above point to the importance of conformational antigenic specificity at various levels and in different regions of the IgM molecule.…”

Section: Discussionsupporting

confidence: 50%

PAPAIN DIGESTION FRAGMENTS OF HUMAN IGM GLOBULINS

Mihaesco

Séligmann

1968

The Journal of Experimental Medicine

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The molecular structure of all classes of immunoglobulins seems to follow a basically similar architectural pattern. Whereas light polypeptide chains (kappa and lambda) represent structural units common to all classes of immunoglobulins, the physicochemical and antigenic properties of heavy chains differ markedly from one class to another. Deutsch and Morton (1) showed that 19S IgM globulins are easily dissociated, by mild reduction and alkylation at neutral pH, into 7-8S subunits. Accordingly, an additional level of molecular organization was assumed for IgM globulins compared to IgG globulins. However, the structure of human IgM globulins has only been partially elucidated and many structural concepts have been inferred from the molecular models proposed for IgG globulins.As first shown by Lapresle (2), enzymatic digestion has proved to be a very useful method for elucidating the structure of globular proteins. The physicochemical and immunological study of proteolytic fragments, in which configuration and biological activity of the intact molecule are preserved as much as possible, has led to valuable information on the structure of rabbit and human IgG globulins. Porter, using activated papain as proteolytic agent, first demonstrated a tripartite structure in rabbit IgG globulin (3).As very few data on the cleavage of IgM globulins by papain and pepsin were available, an investigation of the proteolytic products obtained by these enzymes was undertaken on two WaldenstrSm IgM globulins. The probable relevance of such investigations to the structure-function relationship of IgM antibodies was the major reason for this analysis. In a preliminary report (4), we showed that, although proteolytic products similar to Fab, Fab', and Fc fragments could be obtained, striking differences between IgG and IgM proteolysis were apparent. The present study demonstrates that activated papain produces a high yield of small peptides, a Fab/~ fragment with physicochemical and immunological features analogous to those of the Fab fragment of IgG and a large Fc/~ fragment made of small pieces of/z-chains linked by disulfide bonds.

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Section: Discussionsupporting

confidence: 50%