Holt J C, Yan Z Q, Lu W Q, Stewart G J, Niewiarowski S
Rhône-Poulenc Rorer Biotechnology, Inc., King of Prussia, Pennsylvania 19406.
Proc Soc Exp Biol Med. 1992 Feb;199(2):171-7. doi: 10.3181/00379727-199-43343.
Neutrophil-activating peptide 2 (NAP-2), corresponding to platelet basic protein fragment 25-94, was prepared by chymotryptic digestion of its precursors, low affinity platelet factor 4 or beta-thromboglobulin, followed by purification by high performance liquid chromatography. NAP-2 (0.1-1.5 microns) caused the release of human granulocyte elastase from cytochalasin B-treated neutrophils in a dose-dependent manner. In the same system, beta-thromboglobulin, human platelet factor 4, S-pyridylethyl NAP-2, and platelet basic protein C-terminal fragment (77-94) were inactive, whereas platelet basic protein fragment 22-89 had low, but significant, activity. Sensitive immunological identification of NAP-2 based on nonequilibrium isoelectric focusing and immunoblotting is described.
中性粒细胞激活肽2（NAP - 2），对应于血小板碱性蛋白片段25 - 94，通过对其前体低亲和力血小板因子4或β - 血小板球蛋白进行胰凝乳蛋白酶消化，然后通过高效液相色谱法纯化而制备。NAP - 2（0.1 - 1.5微米）以剂量依赖的方式导致细胞松弛素B处理的中性粒细胞释放人粒细胞弹性蛋白酶。在同一系统中，β - 血小板球蛋白、人血小板因子4、S - 吡啶基乙基NAP - 2和血小板碱性蛋白C末端片段（77 - 94）无活性，而血小板碱性蛋白片段22 - 89具有低但显著的活性。描述了基于非平衡等电聚焦和免疫印迹的NAP - 2的灵敏免疫鉴定方法。
