(A) leech-derived human leukocyte elastase inhibitor = 거머리에서 분리한 단백질 분해 효소 억제제에 관한 연구

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Inhibitory peptides against protease were studied from a Korean native leech species, Hirudo nipponia. An elastase inhibitor was purified and characterized by using Sephadex G-75 gel filtration, anion exchange chromatography on DEAE-Sepharose and $C_{18}$ reversed phase HPLC column, followed by acetone precipitation and the complete amino acid sequence of the inhibitor was determined. The purified peptide has a molecular weight of 6,119 Da on MALDI mass spectrum. Inhibitory activity of the peptide was examined on the various kind of proteases. Though the inhibitory peptide has a small effect on chymotrypsin and subtilisin, no inhibitory effect on other proteases such as trypsin, pepsin, and papain was observed. The peptide is stable at the wide range of pH 1 to 11 and is heat stable up to $90^\circ C$. The sequence of the peptide was compared with other peptide inhibitors. The amino acid sequence of the peptide shows similarity to subtilisin - chymotrypsin inhibitors from barley and maize and Factor Xa inhibitor, antistasin, from Mexican leech.
Advisors
Kang, Ke-Won강계원
Description
한국과학기술원 : 생물공학과,
Publisher
한국과학기술원
Issue Date
1995
Identifier
98710/325007 / 000933472
Language
eng
Description

학위논문(석사) - 한국과학기술원 : 생물공학과, 1995.2, [ v, 47 p. ]

URI
http://hdl.handle.net/10203/28476
Link
http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=98710&flag=dissertation
Appears in Collection
BS-Theses_Master(석사논문)
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