PURIFICATION, SEQUENCE AND ANTIBACTERIAL ACTIVITY OF 2 NOVEL SAPECIN HOMOLOGS FROM SARCOPHAGA EMBRYONIC-CELLS - SIMILARITY OF SAPECIN-B TO CHARYBDOTOXIN

被引：67

作者：

YAMADA, K ^{[1
]}

NATORI, S ^{[1
]}

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN

来源：

BIOCHEMICAL JOURNAL | 1993年 / 291卷

关键词：

D O I：

10.1042/bj2910275

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：

Two sapecin homologues were purified from the culture medium of NIH-Sape-4, an embryonic cell line of Sarcophaga peregrina (flesh fly). These homologues contained six cysteine residues with exactly the same disulphide pairings as those in sapecin. The amino acid sequence of one of them, sapecin C, was also very similar to that of sapecin. The other homologue, sapecin B, was less similar to sapecin but showed significant similarity to charybdotoxin, an inhibitor of K+ channels isolated from a scorpion venom. Like sapecin, these homologues repressed the growth of various Gram-positive bacteria.

引用

页码：275 / 279

页数：5

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