Interaction of concanavalin A with sugar residues of collagen from different tissues.
Topochemical characteristics of reactions of different types of collagen-containing structures with Concanavalin A (Con A) have not been considered up to now. In this study the presence and availability of glucose residues of collagen molecules from intestine, liver, cartilage and tendon are detected using Con A and horseradish peroxidase (HRP). In intestine, cartilage and tendon sections, the Con A-HRP method was only significantly positive when the sections were first submitted to treatment with papain. This suggested the presence of glycoproteins and proteoglycans of the extracellular matrix (ECM), which might interfere either interacting with lateral sugar residues of the collagen molecules, or causing some steric blockade or even masking as occurs in regions with a high state of compactness.
Pimentel
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ER
Departamento de Biologia Celúlar, UNICAMP, SP.
Vidal
E de C
Ede C
D000818:Animals; D002356:Cartilage / Q000378:metabolism; D003094:Collagen / Q000378:metabolism*; D003208:Concanavalin A / Q000378:metabolism*; D005109:Extracellular Matrix / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism*; D006735:Horseradish Peroxidase; D007420:Intestine, Large / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D051381:Rats; D013710:Tendons / Q000378:metabolism
D003208:Concanavalin A; D003094:Collagen; D006735:Horseradish Peroxidase; D005947:Glucose