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KMID : 0545120000100010081
Journal of Microbiology and Biotechnology
2000 Volume.10 No. 1 p.81 ~ p.85
Characterization of an Elastase Inhibitor Produced by Streptomyces lavendulae SMF11
Lee, Hyun Sook
Jin, Wook/Kang, Sung Gyun/Hwang, Yoon Sook/Kho, Yung Hee/Lee, Kye Joon
Abstract
An elastase inhibitor, SMFEI02, was isolated from culture broth of Streptomyces lavendulae SMF11. The inhibitor was purified by ultrafiltration followed by XAD-7 column and Dowex-1 anion-exchange chromatographies, and preparative HPLC. The molecular formula was determined to be C_14H_16N_2O_2 (MW 244) by HRFAB-MS analysis. The inhibitor was identified to be a diketopiperazine cyclo(S-Phe-S-Pro) by the optical rotation value and NMR spectral data, and showed inhibitory activities for trypsin, chymotrypsin, cathepsin B, and papain as well as elastase with the K_i values ranging from 1.78mM to 2.86¥ìM. The inhibition showed a competitive mode for elastase, chymotrypsin, and cathepsin B, whereas it showed a noncompetitive mode for trypsin and papain.
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