Extrinsic Signals for Monitoring the Association Reaction of Proteins as Introduced by Fluorescent and Non-Fluorescent Labels

Extrinsic Signals for Monitoring the Association Reaction of Proteins as Introduced by... Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1283- 1296, September 1976 Bernhard BÖSTLRLING, Jürgen ENGEL, Adrian STEINEMANN and Hans J. SCHRAMM Biozentrum der Universität Basel, Abt. Biophysikalische Chemie und Max-Planck-Institut fur Biochemie, Martinsried bei München (Received 6 May 1976) Summary: Two known dansyl labels (I, II) and 5-[2-(iodoacetamido)ethylamino]-l-naphthalenesulfonic acid (III) and three new azo-dyes (IV-VI) were covalently attached to -chymotrypsin and to basic pancreatic trypsin inhibitor by four different reactive groups. In order to protect the contact region of the proteins the complex of the two proteins was labeled. Advantage was taken of the fact that a group which is buried in the complex reacts about V[C]/K times slower than a group which is always exposed (K = dissociation equilibrium constant, [C] = concentration of the complex). The complex was dissociated at pH 3 and the labeled proteins were isolated by column chromatography. They were fully active. The dansyl label was immobilized when introduced by dansyl chloride but highly mobile when attached via the longer imidoester group (II). Changes of absorption and of fluorescence which occur when differently labeled reaction partners recombine were studied. Changes in absorption (up to 18%) were mainly due to interactions of the label http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png hoppe-seyler's zeitschrift für physiologische chemie de Gruyter

Extrinsic Signals for Monitoring the Association Reaction of Proteins as Introduced by Fluorescent and Non-Fluorescent Labels

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Publisher
de Gruyter
Copyright
Copyright © 1976 by the
ISSN
0018-4888
eISSN
1437-4315
DOI
10.1515/bchm2.1976.357.2.1283
Publisher site
See Article on Publisher Site

Abstract

Hoppe-Seyler's Z. Physiol. Chem. Bd. 357, S. 1283- 1296, September 1976 Bernhard BÖSTLRLING, Jürgen ENGEL, Adrian STEINEMANN and Hans J. SCHRAMM Biozentrum der Universität Basel, Abt. Biophysikalische Chemie und Max-Planck-Institut fur Biochemie, Martinsried bei München (Received 6 May 1976) Summary: Two known dansyl labels (I, II) and 5-[2-(iodoacetamido)ethylamino]-l-naphthalenesulfonic acid (III) and three new azo-dyes (IV-VI) were covalently attached to -chymotrypsin and to basic pancreatic trypsin inhibitor by four different reactive groups. In order to protect the contact region of the proteins the complex of the two proteins was labeled. Advantage was taken of the fact that a group which is buried in the complex reacts about V[C]/K times slower than a group which is always exposed (K = dissociation equilibrium constant, [C] = concentration of the complex). The complex was dissociated at pH 3 and the labeled proteins were isolated by column chromatography. They were fully active. The dansyl label was immobilized when introduced by dansyl chloride but highly mobile when attached via the longer imidoester group (II). Changes of absorption and of fluorescence which occur when differently labeled reaction partners recombine were studied. Changes in absorption (up to 18%) were mainly due to interactions of the label

Journal

hoppe-seyler's zeitschrift für physiologische chemiede Gruyter

Published: Jan 1, 1976

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