AMINO-ACID-SEQUENCE OF CAP37, A HUMAN NEUTROPHIL GRANULE-DERIVED ANTIBACTERIAL AND MONOCYTE-SPECIFIC CHEMOTACTIC GLYCOPROTEIN STRUCTURALLY SIMILAR TO NEUTROPHIL ELASTASE

被引：66

作者：

POHL, J

PEREIRA, HA

MARTIN, NM

SPITZNAGEL, JK

机构：

[1] EMORY UNIV,SCH MED,DEPT MICROBIOL & IMMUNOL,ROLLINS RES CTR,ROOM 3152,ATLANTA,GA 30322

[2] EMORY UNIV,SCH MED,WINSHIP CANC CTR,MICROCHEM FACIL,ATLANTA,GA 30322

来源：

FEBS LETTERS | 1990年 / 272卷 / 1-2期

关键词：

Antibacterial activity; Cationic granule protein; Monocyte chemotaxis; Neutrophil; Serine proteinase;

D O I：

10.1016/0014-5793(90)80484-Z

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：

We report the amino acid sequence of CAP37, a human neutrophil granule protein with antibacterial and monocyte-specific chemotactic activity. CAP37 is a single-chain protein consisting of 222 amino acid residues. It has three N-glycosylation sites, at Asn residues 100, 114 and 145. Some species of CAP37 are glycosylated at all three sites; some at Asn-114 alone, others at Asn-114 and Asn-110 or Asn-145. CAP37 has 45% sequence identity to human neutrophil elastase, and 30-37% identity to several other granule serine proteinases. Despite these similarities, CAP37 is not a serine proteinase because the active site residues serine and histidine are replaced. © 1990.

引用

页码：200 / 204

页数：5

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