Deglycosylation of the chymotryptic collagen‐binding fragment of human plasma fibronectin does not modify its affinity to denatured collagen

FEBS Letters

Delannoy, Philippe¹  Montreuil, Jean¹ 

[1] Laboratoire de Chimie Biologique (Unité Associée au CNRS no. 217), Université des Sciences et Techniques de Lille Flandres-Artois, F-59655 Villeneuve d'Ascq Cedex, France

关键词: Fibronectin;    Collagen;    Peptide-N 4-(N-acetyl-β-glucosaminyl)asparagine amidase;    Glycosylation;    BSA;    bovine serum albumin;    Fn;    fibronectin;    pFn;    human plasma fibronectin;    PMSF;    phenylmethylsulfonyl fluoride;    SDS-PAGE;    SDS-polyacrylamide gel electrophoresis;    TBS;    10 mM Tris-HCl/0.154 M NaCl (pH 7.2) buffer;   

DOI  :  10.1016/0014-5793(89)81232-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown