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PEROXIDASE-LABELED ANTIBODY A NEW METHOD OF CONJUGATION
Journal of Histochemistry & Cytochemistry · 1974 · Vol. 22(12) · pp. 1084–1091
Paul K. Nakane✉(University of Colorado Boulder)Akira Kawaoi(University of Colorado Boulder)
Abstract
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.
Neutrophil, Myeloperoxidase and Oxidative MechanismsViral Infectious Diseases and Gene Expression in InsectsBiochemical effects in animalsPeroxidaseSodium periodateHorseradish peroxidaseChemistryPeriodateBiochemistryMoietyEnzymeAldehydeAntibody
MeSH terms
AnimalsAntibodiesAntigen-Antibody ReactionsBorohydridesHistocytochemistryImmunoglobulin GNitrobenzenesPeroxidasesRabbitsSheepMice
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2,352
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References
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Journal of Organometallic Chemistry · 1976 · 2,346 citations
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