13C NMR studies of the binding of soybean trypsin inhibitor to trypsin. |
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Authors: | M W Hunkapiller M D Forgac E H Yu J H Richards |
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Affiliation: | Contribution #5952, Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125 USA |
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Abstract: | NMR studies of the complex between trypsin and soybean trypsin inhibitor with 1-13C-arginine and modified inhibitor with 1-13C-lysine show that these complexes involve almost exclusively non-covalent binding of the inhibitor to the enzyme for trypsin/13C-Lys-inhibitor at pH 6.5 and 8.1 and for trypsin/13C-Arg-inhibitor at pH 5.0. At pH 7.1 for trypsin/13C-Arg-inhibitor both non-covalent and acyl enzyme forms are observed. Under no conditions did we observe evidence for a tetrahedral adduct between enzyme and inhibitor. |
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