Concanavalin A-horseradish peroxidase bridge staining of alpha-1 glycoproteins separated by isoelectric focusing on polyacrylamide gel. | Zendy

Robert C. Allen | Zendy; S. S. Spicer | Zendy; David R. Zehr | Zendy

Open Access

Concanavalin A-horseradish peroxidase bridge staining of alpha-1 glycoproteins separated by isoelectric focusing on polyacrylamide gel.

Author(s) -

Robert C. Allen,

S. S. Spicer,

David R. Zehr

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 - 10.1177/24.8.60439

Subject(s) - horseradish peroxidase , isoelectric focusing , concanavalin a , glycoprotein , staining , chemistry , chromatography , peroxidase , polyacrylamide gel electrophoresis , isoelectric point , polyacrylamide , biochemistry , mannose , stain , microbiology and biotechnology , biology , enzyme , polymer chemistry , in vitro , genetics

The Coomassie Blue protein stain and the periodic acid-Schiff stain for glycoproteins are compared to a new method of staining glycoproteins resolved electrophoretically. The method utilizes a Concanavalin A-horseradish peroxidase sequence to visualize selectively glycoproteins with terminal or internal mannose or terminal N-acetylglucosamine. The method applied to characterization of M and Z allele products of alpha-l-antitrypsins separated by isoelectric focusing of polyacrylamide gels slabs have revealed differences in carbohydrate content of various components that were previously undetected.

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