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Trypsin‐SBTI interaction in reverse micelles A slow intermicellar exchange‐dependent binding
Author(s) -
Bru Roque,
Garcia-Carmona Francisco
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80470-n
Subject(s) - micelle , chemistry , macromolecule , trypsin , pulmonary surfactant , aqueous solution , chromatography , biophysics , organic chemistry , enzyme , biochemistry , biology
Solubilisate exchange between reverse micelles must take place before any reaction inside reverse micelles occurs if the reactants are confined to the aqueous micellar core. When the interacting species are 2 small molecules or one small molecule and one macromolecule, it has been shown that the exchange is faster than the typical turnover of an enzymatic reaction. The study of the interaction between 2 macromolecules (trypsin and soybean trypsin inhibitor) in reverse micelles carried out in this work reveals that the exchange between these macromolecule‐containing reverse micelles slows down by a thousand times and the limiting‐step in the exchange, the fusion, by 10* times. Both reverse micellar size (ω o = [water]/ [surfactant]) and temperature affected the rate of the fusion process. A hypothesis for the proposed active role of macromolecules in the exchange process is also given.