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The Demonstration of Plasmin Agglutinators in Human Sera 1
Author(s) -
Waller M.,
Curry N.
Publication year - 1970
Publication title -
vox sanguinis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.68
H-Index - 83
eISSN - 1423-0410
pISSN - 0042-9007
DOI - 10.1111/j.1423-0410.1970.tb01493.x
Subject(s) - plasmin , papain , chemistry , trypsin , antibody , immunoglobulin fab fragments , biochemistry , elastase , chymotrypsin , microbiology and biotechnology , titer , immunoglobulin fc fragments , hydrolysis , pepsin , enzyme , immunoglobulin g , biology , peptide sequence , immunology , gene , complementarity determining region
Plasmin agglutinators are natural IgG anti‐Fab antibodies. These antibodies bind to erythrocytes which are coated with the Fab fragments of anti‐Rh antibodies that have been hydrolyzed with plasmin. The plasmin agglutinators are demonstrable in most human sera albeit in low titer. These agglutinators can be inhibited with Fab fragments that have been hydrolyzed with subtilisin, bromelin, trypsin, and plasmin but cannot be inhibited by Fab fragments from pepsin, ficin, chymotrypsin, papain or elastase digests. The Fab fragments from naturally fragmented immune serum globulin gave identical inhibition reactions to those produced by plasmin hydrolysis.