Vorland L H, Ulvatne H, Andersen J, Haukland H, Rekdal O, Svendsen J S, Gutteberg T J
Department of Medical Microbiology, University Hospital, Tromsø, Norway.
Scand J Infect Dis. 1998;30(5):513-7. doi: 10.1080/00365549850161557.
The antimicrobial peptide lactoferricin is generated by gastric pepsin cleavage of lactoferrin. We have examined the antimicrobial activity of lactoferricins derived from lactoferrin of human, murine, caprine and bovine origin with minimal inhibitory concentration (MIC) and minimal bactericidal concentration (MBC) against E. coli ATCC 25922 and S. aureus ATCC 25923. We found that lactoferricin of bovine origin (Lf-cin B) was the most efficacious of the lactoferricins tested. By comparing the linear and cyclic Lf-cin B we found the cyclic peptide to be the most active. Lactoferricin B was moderately active against E. coli ATCC 25922 and S. aureus ATCC 25923, but had no activity against P. mirabilis or Y. enterocolitica. Lf-cin B showed good activity against C. albicans, C. tropicalis and C. neoformans.
抗菌肽乳铁传递素是由胃蛋白酶切割乳铁蛋白产生的。我们用最小抑菌浓度（MIC）和最小杀菌浓度（MBC）检测了源自人、鼠、羊和牛乳铁蛋白的乳铁传递素对大肠杆菌ATCC 25922和金黄色葡萄球菌ATCC 25923的抗菌活性。我们发现牛源乳铁传递素（Lf-cin B）在测试的乳铁传递素中最有效。通过比较线性和环状Lf-cin B，我们发现环状肽活性最强。乳铁传递素B对大肠杆菌ATCC 25922和金黄色葡萄球菌ATCC 25923有中等活性，但对奇异变形杆菌或小肠结肠炎耶尔森菌无活性。Lf-cin B对白色念珠菌、热带念珠菌和新型隐球菌显示出良好活性。
