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
hoppe-seyler's zeitschrift für physiologische chemie – de Gruyter
Published: Jan 1, 1976
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