首页> 外文期刊>Scandinavian journal of infectious diseases. >Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin.
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Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin.

机译:牛源乳铁蛋白比人源,鼠源和鼠源性乳铁蛋白的活性更高。

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摘要

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.
机译:抗菌肽乳铁蛋白是通过胃胃蛋白酶切割乳铁蛋白而产生的。我们检查了源自人,鼠,鼠和牛的乳铁蛋白的乳铁蛋白的抑菌活性,其对大肠杆菌ATCC 25922和金黄色葡萄球菌ATCC 25923的最小抑菌浓度(MIC)和最小杀菌浓度(MBC)。我们发现牛源乳铁蛋白(Lf-cin B)在所测试的乳铁蛋白中最有效。通过比较线性和环状Lf-cin B,我们发现环状肽是最有活性的。乳铁蛋白B对大肠杆菌ATCC 25922和金黄色葡萄球菌ATCC 25923具有中等活性,但对拟南芥假单胞菌或小肠结肠炎耶尔森氏菌没有活性。 Lf-cin B对白色念珠菌,热带念珠菌和新形态梭菌显示出良好的活性。

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