Schröder J M, Sticherling M, Persoon N L, Christophers E
Department of Dermatology, University of Kiel, Federal Republic of Germany.
Biochem Biophys Res Commun. 1990 Oct 30;172(2):898-904. doi: 10.1016/0006-291x(90)90760-k.
A novel protein, NAP-4, could be isolated from human platelet lysates. NAP-4 preparations induced chemotaxis of human neutrophils with an ED50 near 400 ng/ml. Purification by anti NAP-1/IL-8 affinity chromatography and reversed phase HPLC revealed a single peak showing a single line upon SDS-PAGE corresponding to a Mr of 8000. NH2-terminal sequence analysis indicated an unique sequence showing strong homology to human platelet factor 4 and weak homology to tumor necrosis factor alpha as well. The most interesting finding is the absence of the first two cysteins, known to be strongly conserved in members of the family of platelet-factor 4-like host defense cytokines.
一种新型蛋白质，即NAP-4，可以从人血小板裂解物中分离出来。NAP-4制剂可诱导人中性粒细胞趋化，其半数有效剂量（ED50）接近400 ng/ml。通过抗NAP-1/IL-8亲和色谱和反相高效液相色谱纯化后，在SDS-PAGE上显示出一个单峰，对应于8000的分子量。氨基末端序列分析表明，其具有独特的序列，与人类血小板因子4有很强的同源性，与肿瘤坏死因子α也有较弱的同源性。最有趣的发现是，在血小板因子4样宿主防御细胞因子家族成员中，已知高度保守的前两个半胱氨酸缺失。
