多胺与人血浆蛋白的相互作用：纤维蛋白原和纤连蛋白（冷不溶性球蛋白）的优先聚集。

Interaction of polyamines with proteins of human plasma: a preferential aggregation of fibrinogen and fibronectin (cold insoluble globulin).

作者信息

Vuento M, Salonen E, Riepponen P

出版信息

Biochimie. 1980;62(1):99-104. doi: 10.1016/s0300-9084(80)80376-2.

Abstract

The polyamines spermine and spermidine were found to aggregate proteins from human plasma and serum, apparently due to electrostatic interactions between these cations and anionic proteins. Fibrinogen and fibronectin (cold insoluble globulin) were identified as the major molecular components of aggregates, and fibronectin could be quantitatively removed from plasma by aggregation with spermine. The results indicate that fibrinogen and fibronectin have anionic groups which react with polyamines and which are essential for the solubility of these proteins.

摘要

已发现多胺精胺和亚精胺会使来自人血浆和血清的蛋白质聚集，这显然是由于这些阳离子与阴离子蛋白质之间的静电相互作用所致。纤维蛋白原和纤连蛋白（冷不溶性球蛋白）被确定为聚集体的主要分子成分，并且通过与精胺聚集，纤连蛋白可从血浆中被定量去除。结果表明，纤维蛋白原和纤连蛋白具有与多胺反应的阴离子基团，且这些基团对于这些蛋白质的溶解性至关重要。