NEW INTRAMOLECULARLY QUENCHED FLUOROGENIC PEPTIDE-SUBSTRATES FOR THE STUDY OF THE KINETIC SPECIFICITY OF PAPAIN

被引：44

作者：

GARCIAECHEVERRIA, C

RICH, DH

机构：

[1] UNIV WISCONSIN,SCH PHARM,425 N CHARTER ST,MADISON,WI 53706

[2] UNIV WISCONSIN,DEPT CHEM,MADISON,WI 53706

来源：

FEBS LETTERS | 1992年 / 297卷 / 1-2期

关键词：

CYSTEINE PROTEINASE; PAPAIN; FLUORESCENCE; RESONANCE ENERGY TRANSFER;

D O I：

10.1016/0014-5793(92)80336-F

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A series of new substrates for determining the catalytic activity of cysteine proteinases is described. The rate of hydrolysis by papain was monitored by a fluorescence continuous assay based on internal resonance energy transfer using 5-[(2-aminoethyl)amino]naphtalene-1-sulfonic acid (EDANS) and 4-(4-dimethylaminophenylazo)benzoic acid (DABCYL) as fluorescent donor and quenching acceptor, respectively, in peptides with the general structure: DABCYL-Lys-Phe-Gly-Xxx-Ala-Ala-EDANS. The substrates were used to evaluate the effect of amino acid structure in the S1' position on the kinetic parameters for papain catalyzed hydrolysis.

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收藏

页码：100 / 102

页数：3

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