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Intrinsic fluorescence of enzymes and fluorescence of chemically modified enzymes for analytical purposes: a review
Author(s) -
Galbán Javier,
Andreu Yolanda,
Sierra Jose F.,
de Marcos Susana,
Castillo Juan R.
Publication year - 2001
Publication title -
luminescence
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.428
H-Index - 45
eISSN - 1522-7243
pISSN - 1522-7235
DOI - 10.1002/bio.633
Subject(s) - fluorophore , fluorescence , enzyme , chemistry , substrate (aquarium) , covalent bond , combinatorial chemistry , photochemistry , biochemistry , organic chemistry , optics , physics , biology , ecology
In recent years our research group has developed new alternatives for fluorescence enzymatic determinations. First, we observed that the intrinsic fluorescence of enzymes changes during enzymatic reactions, proportionally to the substrate concentration, avoiding the combination of the enzymatic reaction with a fluorophore‐involving reaction. The main disadvantage of this method is that the excitation and emission wavelengths of the enzymes are in the UV region of the spectrum. An alternative to overcome this problem consisted of covalently bonding the enzyme to a fluorophore. In this paper, an overview is given of all of the applications and future developments on both types of alternatives that we have developed. Apart from the analytical charactersitics of the methods, we have also reviewed all of the information about mathematical models we have elaborated to date. Copyright © 2001 John Wiley & Sons, Ltd.