Garnotel R, Wegrowski J, Bellon G, Monboisse J C, Perreau C, Borel J P
Laboratory of Biochemistry, CNRS ERS 0017, Faculty of Medicine, University of Reims-Champagne Ardenne, Reims, France.
Exp Cell Res. 1993 Apr;205(2):426-9. doi: 10.1006/excr.1993.1109.
After separation of the various alpha chains of the collagens by SDS-PAGE, the binding of polymorphonuclear neutrophils (PMN) to these chains was detected by a double-antibody technique and the activation of PMN by nitro blue tetrazolium. All of the alpha chains tested were able to bind PMNs. The alpha 1 chain of type I collagen activated the PMN when it had not been treated with pepsin. Pepsinized types II and VI collagens did not activate PMN. The pepsinized alpha 1(III) chains and all three alpha chains from pepsinized type V collagen were able to activate PMN.
通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）分离出胶原蛋白的各种α链后，采用双抗体技术检测多形核中性粒细胞（PMN）与这些链的结合情况，并通过硝基蓝四氮唑检测PMN的激活情况。所有测试的α链都能够结合PMN。未经胃蛋白酶处理的I型胶原蛋白α1链可激活PMN。经胃蛋白酶处理的II型和VI型胶原蛋白不会激活PMN。经胃蛋白酶处理的α1(III)链以及经胃蛋白酶处理的V型胶原蛋白的所有三条α链都能够激活PMN。
