Purification of amoebolytic substances from Bacillus licheniformis M-4.
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.
Lebbadi
M
M
Department of Microbiology, Faculty of Sciences, University of Granada, Spain.
Gálvez
A
A
Valdivia
E
E
Martínez-Bueno
M
M
Maqueda
M
M
D000563:Amebicides / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D001407:Bacillus / Q000378:metabolism*; D009253:Naegleria / Q000187:drug effects / Q000254:growth & development; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism / Q000494:pharmacology
D000563:Amebicides; D010455:Peptides