PURIFICATION OF AMOEBOLYTIC SUBSTANCES FROM BACILLUS-LICHENIFORMIS M-4

被引：0
|
作者：
LEBBADI, M
GALVEZ, A
VALDIVIA, E
MARTINEZBUENO, M
MAQUEDA, M
机构：
[1] UNIV JAEN,FAC CIENCIAS EXPTL,DEPT MICROBIOL,E-23071 JAEN,SPAIN
[2] UNIV GRANADA,FAC SCI,DEPT MICROBIOL,E-18071 GRANADA,SPAIN
来源：
ARCHIVES OF MICROBIOLOGY | 1994年 / 162卷 / 1-2期
关键词：
AMOEBICIN; ANTIBIOTIC; BACILLUS LICHENIFORMIS; NAEGLERIA;
D O I：
暂无
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
Three antibiotic peptides with amoebolytic activity have been purified from culture supernatants of Bacillus licheniformis M-4 (amoebicins m4-A, m4-B, and m4-C). They were hydrophilic peptides consisting of six different amino acids (Asp, Glu, Ser, Thr, Pro, Tyr). Their molecular weights ranged from 3,000 to 3,200. Purified amoebicins were active against human pathogenic and non-pathogenic strains of Naegleria. They also showed a broad antifungal spectrum, but a narrow antibacterial activity.
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页码：98 / 102
页数：5
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