Deglycosylation of the chymotryptic collagen-binding fragment of human plasma fibronectin does not modify its affinity to denatured collagen.
N-Glycanase deglycosylation of purified 44 kDa chymotryptic collagen-binding domain from human plasma fibronectin does not significantly modify its behavior on gelatin affinity chromatography. This indicates that carbohydrates do not play any role in the binding affinity of fibronectin to collagen. The influence of changes in glycosylation on the biological functions of fibronectin is discussed.
Delannoy
P
P
Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Villenuve d'Ascq, France.
Montreuil
J
J
D001665:Binding Sites; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D002918:Chymotrypsin / Q000378:metabolism*; D003094:Collagen / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005353:Fibronectins / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006031:Glycosylation; D006801:Humans; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism*; D011489:Protein Denaturation
D005353:Fibronectins; D010446:Peptide Fragments; D003094:Collagen; D006026:Glycoside Hydrolases; C020668:glycanase; D002918:Chymotrypsin