期刊
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 53, 期 16, 页码 6491-6496出版社
AMER CHEMICAL SOC
DOI: 10.1021/jf0505123
关键词
antifungal protein J (AFP-J); potato; serine protease inhibitor; Kunitz family
An antifungal protein, AFP-J, was purified from tubers of the potato (Solanum tuberosum cv. L Jopung) by various chromatographic columns. AFP-J strongly inhibited yeast fungal strains, including Candida albicans, Trichosporon beigelii, and Saccharomyces cerevisiae, whereas it exhibited no activity against crop fungal pathogens. Automated Edman degradation determined the partial N-terminal sequence of AFP-J to be NH2-Leu-Pro-Ser-Asp-Ala-Thr-Leu-Val-Leu-Asp-Gln-Thr-Gly-Lys-G Iu-Leu-Asp-Ala-Arg-Leu-. The partially sequence had 83% homology with a serine protease inhibitor belonging to the Kunitz family, and the protein inhibited chymotrypsin, pepsin, and trypsin. Mass spectrometry showed that its molecular mass was 13 500.5 Da. This protease inhibitor suppressed over 50% the proteolytic activity at 400 mu g/mL. These results suggest that AFP-J is an excellent candidate as a lead compound for the development of novel antiinfective agents.
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