Yamaguchi Y, Isemura M, Yosizawa Z, Sato A, Suzuki M
Tohoku J Exp Med. 1983 Nov;141(3):359-67. doi: 10.1620/tjem.141.359.
Human fibronectins isolated from pooled human plasma and amniotic fluid were studied as to differences in their carbohydrate moieties. The chemical analyses showed that amniotic fluid fibronectin is different from adult plasma fibronectin in carbohydrate content and composition while there seems to be no significant differences in amino acid composition. Crossed immunoaffinity electrophoresis with free concanavalin A, as well as rocket immunoelectrophoresis with immobilized concanavalin A intermediate gel, indicated that amniotic fluid fibronectin has little or no reactivity with this lectin while adult plasma fibronectin is strongly reactive. Fetal cord plasma fibronectin apparently interacted with concanavalin A, but its reactivity was weaker than that of adult plasma fibronectin. Fibronectin isolated from ascitic fluid of an ovarian cancer patient which was examined in additional experiments showed much weaker Con A-reactivity than fetal cord plasma fibronectin. These results suggest that fibronectins from various body fluids differ in their carbohydrate structures.
对从混合人血浆和羊水中分离出的人纤连蛋白的碳水化合物部分差异进行了研究。化学分析表明，羊水纤连蛋白在碳水化合物含量和组成上与成人血浆纤连蛋白不同，而氨基酸组成似乎没有显著差异。用游离伴刀豆球蛋白A进行交叉免疫亲和电泳，以及用固定化伴刀豆球蛋白A中间凝胶进行火箭免疫电泳，表明羊水纤连蛋白与这种凝集素几乎没有或没有反应性，而成人血浆纤连蛋白具有强烈反应性。胎儿脐带血浆纤连蛋白显然与伴刀豆球蛋白A相互作用，但其反应性比成人血浆纤连蛋白弱。在额外实验中检测的从一名卵巢癌患者腹水中分离出的纤连蛋白显示，其伴刀豆球蛋白A反应性比胎儿脐带血浆纤连蛋白弱得多。这些结果表明，来自各种体液的纤连蛋白在碳水化合物结构上存在差异。
