PEROXIDASE-LABELED ANTIBODY A NEW METHOD OF CONJUGATION
Author(s) -
Paul K. Nakane,
Akira Kawaoi
Publication year - 1974
Publication title -
journal of histochemistry and cytochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.971
H-Index - 124
eISSN - 1551-5044
pISSN - 0022-1554
DOI - 10.1177/22.12.1084
Subject(s) - peroxidase , sodium periodate , horseradish peroxidase , chemistry , periodate , biochemistry , moiety , enzyme , aldehyde , antibody , chromatography , stereochemistry , organic chemistry , biology , immunology , catalysis
A new method of conjugating horseradish peroxidase with proteins was developed. The carbohydrate moiety of fluorodinitrobenzene-blocked peroxidase was oxidized with sodium periodate to form aldehyde groups. The peroxidase-aldehyde was then bound to free amino groups of proteins unidirectionally at high efficiencies. Peroxidase-labeled immunoglobulin retained its immunologic as well as enzymatic activities.
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