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^(13)C NMR studies of the binding of soybean trypsin inhibitor to trypsin

Hunkapiller, Michael W. and Forgac, Michael D. and Yu, Ellen Ho and Richards, John H. (1979) ^(13)C NMR studies of the binding of soybean trypsin inhibitor to trypsin. Biochemical and Biophysical Research Communications, 87 (1). pp. 25-31. ISSN 0006-291X. doi:10.1016/0006-291X(79)91642-5.

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NMR studies of the complex between trypsin and soybean trypsin inhibitor with 1-^(13)C-arginine and modified inhibitor with 1-^(13)C-lysine show that these complexes involve almost exclusively non-covalent binding of the inhibitor to the enzyme for trypsin/^(13)C-Lys-inhibitor at pH 6.5 and 8.1 and for trypsin/^(13)C-Arg-inhibitor at pH 5.0. At pH 7.1 for trypsin/^(13)C-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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Additional Information:© 1979 by Academic Press. Inc. Received 17 January 1979. This work was supported by NIH grants GM 10218 and GM 16424.
Funding AgencyGrant Number
NIHGM 10218
NIHGM 16424
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Caltech Division of Chemistry and Chemical Engineering5952
Issue or Number:1
Record Number:CaltechAUTHORS:20150428-071027468
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Official Citation:Michael W. Hunkapiller, Michael D. Forgac, Ellen Ho Yu, John H. Richards, 13C NMR studies of the binding of soybean trypsin inhibitor to trypsin, Biochemical and Biophysical Research Communications, Volume 87, Issue 1, 15 March 1979, Pages 25-31, ISSN 0006-291X, (
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ID Code:57030
Deposited On:28 Apr 2015 19:15
Last Modified:10 Nov 2021 21:07

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