COMPLEMENTARY-DNA SEQUENCE OF RABBIT CAP18 - A UNIQUE LIPOPOLYSACCHARIDE BINDING-PROTEIN

被引：122

作者：

LARRICK, JW ^{[1
]}

MORGAN, JG ^{[1
]}

PALINGS, I ^{[1
]}

HIRATA, M ^{[1
]}

YEN, MH ^{[1
]}

机构：

[1] IWATE MED UNIV,DEPT BACTERIOL,MORIOKA,IWATE 020,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 179卷 / 01期

关键词：

D O I：

10.1016/0006-291X(91)91350-L

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：

CAP18 is a novel 18 kDa cationic protein [pl ≈ 10] originally purified from rabbit granulocytes using as an assay the agglutination of lipopolysaccharide (LPS) coated erythrocytes. cDNA clones encoding CAP18 were isolated from a rabbit bone marrow cDNA library using a PCR generated oligonucleotide probe derived from the N-terminal amino acid sequence. The deduced amino acid sequence reveals a putative signal sequence of 29 amino acids and a mature protein of 142 amino acid residues. The predicted size of the encoded protein is 16.6 kDa with a pl of 10. There are no N-linked glycosylation sites. The CAP18 sequence bears no homology with other known LPS-binding proteins including human bacterial permeability increasing protein (BPI)(1) and rabbit LPS binding protein (LBP)(2). © 1991.

引用

页码：170 / 175

页数：6

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