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Amino acid sequence of the variable region of heavy chain in immunoglobulin (Mot) having unusual papain cleavage sites.

Abstract：

:An IgGl(lambda) Mot myeloma protein showed a unique susceptibility toward papain digestion. The Fab fragment of Mot was more digestible with papain than the Fc fragment. This phenomenon was found to occur by unusual cleavage of the Fd fragment with papain. Determination of the complete primary structure of the V region of the H chain of Mot identified two papain cleavage sites in the second complementarity-determining region (CDR). Amino acid sequence of the cleavage sites was Ser(55)-Asp-Asp-Argdecrease-Thr-Thr-Tyr-Gly-Pro-Argdecrease- Ser-Gln- (decrease = cleavage site). In the vicinity of these cleavage sites, many hydrophilic and polar residues are present and the predicted secondary structure near these cleavage sites suggested that this region was exposed on the surface of the molecule, and that the unusual papain cleavage of the IgG Mot might be caused by a unique conformation of the molecule, making it highly susceptible to enzyme digestion.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Kojima M,Koide T,Odani S,Ono T

doi

10.1016/0161-5890(86)90039-8

subject

Has Abstract

pub_date

1986-02-01 00:00:00

pages

169-74

issue

2

eissn

0161-5890

issn

1872-9142

journal_volume

23

pub_type

杂志文章

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