PURIFICATION AND CHARACTERIZATION OF A DIPTERICIN HOMOLOG FROM SARCOPHAGA-PEREGRINA (FLESH FLY)

被引:40
作者
ISHIKAWA, M [1 ]
KUBO, T [1 ]
NATORI, S [1 ]
机构
[1] UNIV TOKYO,FAC PHARMACEUT SCI,BUNKYO KU,TOKYO 113,JAPAN
关键词
D O I
10.1042/bj2870573
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
A protein with a molecular mass of 8 kDa was found to be synthesized specifically when the fat-body from injured Sarcophaga peregrina larvae was cultured in vitro. This protein was purified from the haemolymph of the injured larvae to near-homogeneity. Partial amino acid sequencing revealed that this protein is a diptericin homologue. It showed bactericidal activity on growing, but not resting Escherichia coli cells. E. coli cells become elongated on treatment with this protein.
引用
收藏
页码:573 / 578
页数:6
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