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KMID : 1161420100130061532
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Journal of Medicinal Food
2010 Volume.13 No. 6 p.1532 ~ p.1536
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A New Fibrinolytic Enzyme (55?kDa) from Allium tuberosum: Purification, Characterization, and Comparison
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Chung Dong-Min
Choi Nack-Shick
Chun Hyo-Kon
Maeng Pil-Jae
Park Sang-Bong
Kim Sung-Ho
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Abstract
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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.
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KEYWORD
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Allium tuberosum, fibrin zymography, fibrinolytic enzyme, thrombolytic agent
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