人血浆纤连蛋白胰凝乳蛋白酶胶原结合片段的去糖基化不会改变其与变性胶原的亲和力。
Deglycosylation of the chymotryptic collagen-binding fragment of human plasma fibronectin does not modify its affinity to denatured collagen.
作者信息
Delannoy P, Montreuil J
机构信息
Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Villenuve d'Ascq, France.
出版信息
FEBS Lett. 1989 Apr 10;247(1):25-7. doi: 10.1016/0014-5793(89)81232-3.
PMID:2707448
Abstract
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.
摘要
对人血浆纤连蛋白中纯化的44 kDa胰凝乳蛋白酶胶原结合结构域进行N-聚糖酶去糖基化处理，并不会显著改变其在明胶亲和色谱上的行为。这表明碳水化合物在纤连蛋白与胶原的结合亲和力中不发挥任何作用。文中讨论了糖基化变化对纤连蛋白生物学功能的影响。
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