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与血浆纤连蛋白相比,羊水纤连蛋白具有较弱的明胶结合亲和力和增加的糖基化。

A weaker gelatin-binding affinity and increased glycosylation of amniotic fluid fibronectin than plasma fibronectin.

作者信息

Yamaguchi Y, Isemura M, Yosizawa Z, Kan M, Sato A

出版信息

Int J Biochem. 1986;18(5):437-43. doi: 10.1016/0020-711x(86)90186-2.

Abstract

Human amniotic fluid fibronectin had different carbohydrate moieties from plasma fibronectin. Nearly 90% of glycopeptides released from amniotic fluid fibronectin was not bound by concanavalin A-Sepharose, whereas 75% of glycopeptides from plasma fibronectin was bound. Amniotic fluid fibronectin showed a significantly lower gelatin-binding affinity than plasma fibronectin at 25 degrees C. When the incubation temperature was lowered to 4 degrees C, no significant difference in this activity was found. Cell-attachment promoting activity of the two fibronectins was not significantly different.

摘要

人羊水纤连蛋白与血浆纤连蛋白具有不同的碳水化合物部分。从羊水纤连蛋白释放的糖肽中,近90%不与伴刀豆球蛋白A - 琼脂糖结合,而血浆纤连蛋白的糖肽中有75%与之结合。在25℃时,羊水纤连蛋白显示出比血浆纤连蛋白显著更低的明胶结合亲和力。当孵育温度降至4℃时,该活性未发现显著差异。两种纤连蛋白的细胞附着促进活性没有显著差异。

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