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循环人血浆纤连蛋白的生化与功能异质性。

The biochemical and functional heterogeneity of circulating human plasma fibronectin.

作者信息

Boughton B J, Simpson A W

出版信息

Biochem Biophys Res Commun. 1984 Mar 30;119(3):1174-80. doi: 10.1016/0006-291x(84)90899-4.

DOI:10.1016/0006-291x(84)90899-4
PMID:6712671
Abstract

Human plasma fibronectin purified by affinity chromatography, consisted of homogeneous 215 kD protein subunits when assessed by SDS polyacrylamide gel electrophoresis. On isoelectric focusing however, 5 separate fractions were present, with isoelectric points ranging from 5.6 to 6.1. Isoelectric focusing and immunofixation of native plasma produced similar but not identical appearances. Only 15% of the total plasma fibronectin opsonically stimulated the ingestion of Saccharomyces cerevisiae by human peripheral blood monocytes, and this opsonic fibronectin was confined to the fraction with an isoelectric point of 6.1.

摘要

通过亲和层析纯化的人血浆纤连蛋白,经十二烷基硫酸钠聚丙烯酰胺凝胶电泳评估,由均一的215kD蛋白质亚基组成。然而,在等电聚焦时,出现了5个分离的组分,等电点范围为5.6至6.1。天然血浆的等电聚焦和免疫固定产生了相似但不完全相同的图谱。人血浆纤连蛋白总量中只有15%能通过调理作用刺激人外周血单核细胞摄取酿酒酵母,且这种具有调理作用的纤连蛋白局限于等电点为6.1的组分中。

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