NEUTROPHIL ACTIVATING PEPTIDE-2 BINDS WITH 2 AFFINITIES TO RECEPTOR(S) ON HUMAN NEUTROPHILS

被引：16

作者：

SCHNITZEL, W ^{[1
]}

GARBEIS, B ^{[1
]}

MONSCHEIN, U ^{[1
]}

BESEMER, J ^{[1
]}

机构：

[1] SANDOZ GMBH,A-1235 VIENNA,AUSTRIA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 180卷 / 01期

关键词：

aa; amino acids; PMN; polymorphonuclear leukocytes;

D O I：

10.1016/S0006-291X(05)81292-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Neutrophil receptor(s) for neutrophil activating peptides 1 and 2 were studied by competition binding experiments with radiolabeled NAP-1 and NAP-2 preparations. NAP-1 bound with one affinity, NAP-2 with two quite different affinities, to common receptor(s) on neutrophils. Concentrations of NAP-2 needed to induce exocytosis of β-glucosaminidase corresponded to the higher dissociation constant of the two binding equilibria. Thus, the binding of NAP-2 to PMN with high affinity does not activate the cells. © 1991 Academic Press, Inc.

引用

页码：301 / 307

页数：7

共 8 条

[1] MEASUREMENT OF SPECIFIC RADIOACTIVITIES IN LABELED HORMONES BY SELF-DISPLACEMENT ANALYSIS [J].