Earticle

초록

영어

N,N′-diBoc-dityrosine (DBDY) was conjugated with two molecules of glycine and isoniazid (INH), and tested as a substrate for the protease assay. In DBDY-(Gly-INH)2 and DBDY-(Lys-INH)2, the fluorescence of DBDY (λex=284~320 nm; λem=400~420 nm) disappeared due to the quenching effect of INH. However, the fluorescence recovered upon the protease-catalyzed hydrolysis leading to the release of INH. When cysteine proteases (papain, chymopapain, and bromelain), serine proteases (chymotrypsin, trypsin, subtilisin, and proteinase K), metalloproteases (thermolysin and carboxypeptidase A, dispase, and collagenase), and aspartic proteases (pepsin and aspergillopepsin) were chosen and tested, DBDY-(Gly-INH)2 and DBDY-(Lys-INH)2 showed the selectivity to the cysteine proteases. Cathepsins B, L, and S are classified as the cysteine proteases and have gained lots of interest because they are found at high levels in various cancers. When DBDY-(Gly-INH)2 and DBDY- (Lys-INH)2 were tested as a substrate for these cathepsins, cathepsin B and cathepsin L catalyzed the hydrolysis reaction except cathepsin S.

키워드

저자

• Chan-Jin KIM [ Department of Chemical and Biomolecular Engineering, Yonsei University, Seoul 120-749. ]
• Dong-Ik LEE [ Department of Chemical and Biomolecular Engineering, Yonsei University, Seoul 120-749. ]
• Dong ZHANG [ Department of Chemical and Biomolecular Engineering, Yonsei University, Seoul 120-749. ]
• Ik-Sung AHN [ Department of Chemical and Biomolecular Engineering, Yonsei University, Seoul 120-749. ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576