Peroxidase-conjugate chromatography isolation of conjugates prepared with glutaraldehyde or periodate using polyacrylamide-agarose gel. | Zendy

D. M. Boorsma | Zendy; J.G. Streefkerk | Zendy

Open Access

Peroxidase-conjugate chromatography isolation of conjugates prepared with glutaraldehyde or periodate using polyacrylamide-agarose gel.

Author(s) -

D. M. Boorsma,

J.G. Streefkerk

Publication year - 1976

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 - 10.1177/24.3.177698

Subject(s) - horseradish peroxidase , glutaraldehyde , chromatography , chemistry , periodate , agarose , polyacrylamide , conjugate , sephadex , elution , monomer , potassium periodate , peroxidase , dextran , silica gel , polyacrylamide gel electrophoresis , polymer chemistry , polymer , biochemistry , organic chemistry , enzyme , mathematical analysis , mathematics , detection limit

Fractionation abilities of polyacrylamide-agarose gel (Ultrogel) and dextran gel (Sephadex) column chromatography were compared in isolating horseradish peroxidase conjugates, prepared using two different methods. Utrogel AcA-44 provides an efficient separation of monomer conjugated and nonconjugated immunoglobulins resulting from the two-step glutaraldehyde procedure, Sephadex G-200 does not. Both types of columns eluted the polymer conjugates resulting from the periodate procedure in the void volume; these were hardly isolated from the small amount of monomer conjugate. Unreacted horseradish peroxidase, present in very low quantities after the efficient periodate method and in large amounts after the glutaraldehyde procedure, was separated by both gel types.

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