Histochemical detection of glycogen and glycoconjugates in the inner ear with modified concanavalin A-horseradish peroxidase procedures

1994 ◽  
Vol 26 (5) ◽  
pp. 437-446 ◽  
Author(s):  
Makoto Ito ◽  
Samuel S. Spicer ◽  
Bradley A. Schulte
Keyword(s):  
Horseradish Peroxidase ◽  
Inner Ear ◽  
Concanavalin A ◽  
Histochemical Detection

The origin of centrifugal inner ear fibers of gymnophions (amphibia). A horseradish peroxidase study

1984 ◽  
Vol 46 (2) ◽  
pp. 131-136 ◽  
Author(s):  
Bernd Fritzsch ◽  
Dominique Crapon De Caprona
Keyword(s):  
Horseradish Peroxidase ◽  
Inner Ear

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

1976 ◽  
Vol 24 (8) ◽  
pp. 908-914 ◽  
Author(s):  
R C Allen ◽  
S S Spicer ◽  
D Zehr
Keyword(s):  
Horseradish Peroxidase ◽  
Isoelectric Focusing ◽  
Concanavalin A ◽  
Periodic Acid ◽  
Polyacrylamide Gel ◽  
New Method ◽  
Polyacrylamide Gels ◽  
Periodic Acid Schiff ◽  
Coomassie Blue

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.

A Mediator-free Horseradish Peroxidase Biosensor Based on Concanavalin A

2006 ◽  
Vol 34 (3) ◽  
pp. 399-403 ◽  
Author(s):  
Mengmeng Guo ◽  
Yunhui Yang ◽  
Zhijie Wang ◽  
Guoli Shen ◽  
Ruqin Yu
Keyword(s):  
Horseradish Peroxidase ◽  
Concanavalin A

scholarly journals Histochemical differentiation of complex carbohydrates with variants of the concanavalin A-horseradish peroxidase method.

1978 ◽  
Vol 26 (4) ◽  
pp. 233-250 ◽  
Author(s):  
T Katsuyama ◽  
S S Spicer
Keyword(s):  
Horseradish Peroxidase ◽  
Concanavalin A ◽  
Periodate Oxidation ◽  
Liver Glycogen ◽  
Class Ii ◽  
Class Iii ◽  
Horseradish Peroxidase Method ◽  
Hrp Method ◽  
Complex Carbohydrates ◽  
Mucous Neck Cells

Various treatments carried out prior to the concanavalin A-horseradish perioxidase (HRP) method have been found to affect the staining and have permitted differentiation of three main classes of complex carbohydrates in the rat alimentary tract. Class I mucosubstances lose and class II and III paradoxically gain concanavalin A-horseradish peroxidase reactivity after periodate oxidation. Class II mucosubstances lose whereas class III retain or increase their reactivity with a reduction step interposed between oxidation and concanavalin A-horseradish peroxidase staining. Mucous neck cells, pyloric glands, Brunner's glands and mast cells exhibit strong class III staining, whereas other sites such as intestinal goblet and salivary gland acini differ widely in their type of staining. Liver glycogen stains like mucosubstances in an unstable subgroup of class III. The paradoxical increase in concanavalin A binding during oxidation correlates with the appearance of Schiff reactivity implicating oxidation of vicinal hydroxyls as the basis for the effect. The periodate-induced staining is therefore, thought to result from an oxidative disruption of linkages between vicinal hydroxyls of neighboring sugars and hydroxyls of mannose required for concanavalin A binding. Staining with the described concanavalin A-horseradish peroxidase variants appears to afford information concerning cytochemical distribution of mannose-rich glycoproteins as well as differences among these substances in the relation of mannose to neighboring sugars.

scholarly journals Adsorption of horseradish peroxidase, ovomucoid and anti-immunoglobulin to colloidal gold for the indirect detection of concanavalin A, wheat germ agglutinin and goat anti-human immunoglobulin G on cell surfaces at the electron microscopic level: a new method, theory and application.

1977 ◽  
Vol 25 (11) ◽  
pp. 1187-1200 ◽  
Author(s):  
W D Geoghegan ◽  
G A Ackerman
Keyword(s):  
Horseradish Peroxidase ◽  
Concanavalin A ◽  
Colloidal Gold ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Indirect Detection ◽  
Electron Microscopic Level ◽  
Specific Cell ◽  
Major Protein ◽  
Electron Microscopic

A method is described for the adsorption of selected macromolecules to colloidal gold which is then used as an electron dense marker for the indirect detection of specific cell surface molecules. Membrane bound concanavalin A, which binds specific sugars on horseradish peroxidase, and wheat germ agglutinin, which binds specific sugars on ovomucoid are detected indirectly with gold labeled horseradish peroxidase and ovomucoid, respectively. Goat anti-human IgM on blood lymphocytes is detected with gold labeled rabbit anti-goat IgG. In the preparation of colloidal gold labeled proteins, the problems of flocculation of colloidal gold by proteins and nonadsorption of proteins to colloidal gold, are solved through a combination of concentration of protein and pH variable adsorption isotherms, which allows one to determine the conditions for adsorption of proteins to colloidal gold. Adsorption is pH dependent, the pH conditions correlating with the isoelectric point(s) of the major protein fraction(s); adsorption is influenced by interfacial tension, solubility and by the electrical charge on the molecules. Colloidal gold is inexpensive and preparation of a useful label is rapid, reproducible and the results easily quantitated from electron micrographs.

Staining of Concanavalin A-reactive glycoproteins on polyacrylamide gels with horseradish peroxidase — a critical evaluation

1984 ◽  
Vol 5 (2) ◽  
pp. 77-83 ◽  
Author(s):  
Klaus-Joachim Schott ◽  
Volker Neuhoff ◽  
Birgit Nessel ◽  
Ulla Pötter ◽  
Joachim Schröter
Keyword(s):  
Horseradish Peroxidase ◽  
Concanavalin A ◽  
Critical Evaluation ◽  
Polyacrylamide Gels
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