Abstract
Abstract
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 β-hromboglobulin, followed by purification by high performance liquid chromatography. NAP-2 (0.1–1.5 μm) caused the release of human granulocyte elastase from cytochalasin B-treated neutrophils in a dose-dependent manner. In the same system, β-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.
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