Microbe-Based Fusion Technology Research Center, Jeonbuk Branch Institute, Korea Research Institute of Bioscience and Biotechnology, Jeonbuk, Republic of Korea.
J Med Food. 2010 Dec;13(6):1532-6. doi: 10.1089/jmf.2010.1144. Epub 2010 Oct 18.
Chives have been used both as food and as medicine. Previously, two fibrinolytic enzymes, ATFE-I (90 kDa) and ATFE-II (55 kDa), were identified in chives (Allium tuberosum), a perennial herb. In the present work, ATFE-II was purified by ion-exchange chromatography followed by gel filtration. In addition, the enzyme properties of ATFE-I and ATFE-II were compared. The molecular mass and isoelectric point (pI value) of ATFE-II were 55 kDa and pI 4.0, respectively, as revealed using one- or two-dimensional fibrin zymography. ATFE-II was optimally active at pH 7.0 and 45°C. ATFE-II degraded the Aα-chain of human fibrinogen but did not hydrolyze the Bβ-chain or the γ-chain, indicating that the enzyme is an α-fibrinogenase. The proteolytic activity of ATFE-II was completely inhibited by 1 mM leupeptin, indicating that the enzyme belongs to the cysteine protease class. ATFE-II was also inhibited by 1 mM Fe²(+). ATFE-II exhibited high specificity for MeO-Suc-Arg-Pro-Tyr-p-nitroaniline (S-2586), a synthetic chromogenic substrate of chymotrypsin. Thus proteolytic enzymes from A. tuberosum may be useful as thrombolytic agents.
韭菜既是食物又是药物。先前，在一种多年生草本植物——韭菜（Allium tuberosum）中鉴定出两种纤维蛋白溶酶，ATFE-I（90 kDa）和 ATFE-II（55 kDa）。在本研究中，ATFE-II 通过离子交换层析和凝胶过滤进行纯化。此外，还比较了 ATFE-I 和 ATFE-II 的酶特性。使用一维或二维纤维蛋白电泳发现，ATFE-II 的分子量和等电点（pI 值）分别为 55 kDa 和 pI 4.0。ATFE-II 在 pH 7.0 和 45°C 时具有最佳活性。ATFE-II 降解人纤维蛋白原的 Aα 链，但不水解 Bβ 链或 γ 链，表明该酶是一种 α-纤维蛋白溶酶。ATFE-II 的蛋白水解活性被 1 mM 亮抑酶肽完全抑制，表明该酶属于半胱氨酸蛋白酶类。1 mM Fe²(+)也抑制 ATFE-II。ATFE-II 对 MeO-Suc-Arg-Pro-Tyr-p-硝基苯胺（S-2586）具有高特异性，S-2586 是糜蛋白酶的一种合成显色底物。因此，来自 A. tuberosum 的蛋白水解酶可能可用作溶栓剂。
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