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一种人淋巴细胞衍生的中性粒细胞激活肽(LYNAP)的结构测定

Structure determination of a human lymphocyte derived neutrophil activating peptide (LYNAP).

作者信息

Gregory H, Young J, Schröder J M, Mrowietz U, Christophers E

机构信息

ICI, Pharmaceuticals Division, Macclesfield Cheshire, Great Britain.

出版信息

Biochem Biophys Res Commun. 1988 Mar 15;151(2):883-90. doi: 10.1016/s0006-291x(88)80364-4.

Abstract

Phytohemagglutinin or Concanavalin A-stimulated human T-lymphocytes produce a factor (LYNAP) with potent chemotactic and enzyme degranulating activity in peripheral human neutrophils. Sequence analysis of LYNAP established an apparently novel 72 residue polypeptide structure. Examination of protein data bases showed that LYNAP had about 30% sequence homology with recently characterised connective tissue activating proteins produced by platelets. Furthermore, it was subsequently found that the amino acid sequence is largely the same as that predicted from a cDNA clone derived from mRNA elevated in peripheral human leukocytes stimulated by mitogens.

摘要

植物血凝素或伴刀豆球蛋白A刺激的人T淋巴细胞可产生一种因子(LYNAP),该因子对人外周血中性粒细胞具有强大的趋化活性和酶脱颗粒活性。LYNAP的序列分析确定了一种明显新颖的72个残基的多肽结构。对蛋白质数据库的检查表明,LYNAP与血小板产生的最近鉴定的结缔组织激活蛋白具有约30%的序列同源性。此外,随后发现其氨基酸序列与从有丝分裂原刺激的人外周血白细胞中升高的mRNA衍生的cDNA克隆预测的序列基本相同。

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