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Title 

A new fibrinolytic enzyme (55kDa) from Allium tuberosum: purification, characterization, and comparison

Authors 

Dong Min ChungNack-Shick ChoiHyo Kon ChunP J MaengS B ParkSeung Ho Kim

Publisher 

Mary Ann Liebert

Issue Date 

2010

Citation 

Journal of Medicinal Food, vol. 13, no. 6, pp. 1532-1536

Abstract 

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.

ISSN 

1096-620X

Link 

http://dx.doi.org/10.1089/jmf.2010.1144

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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