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Science 19 July 1968:
Vol. 161. no. 3838, pp. 274 - 276
DOI: 10.1126/science.161.3838.274
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Articles

Conformation and Activity of Chymotrypsin: The pH-Dependent, Substrate-Induced Proton Uptake

James McConn 1, Edmond Ku 1, Catherine Odell 1, George Czerlinski 1, and George P. Hess 1

1 Section of Biochemistry and Molecular Biology, Cornell University, Ithaca, New York 14850

Hydrogen ion uptake by chymotrypsin during reversible binding of specific substrate is shown to be due to an ionizing group of the enzyme with a pK(apparent) sim9 in the free enzyme. This pK(apparent) is shifted to higher value in the enzyme-substrate complexes. Previous results indicating an equilibrium, controlled by this ionizing group, between active and inactive conformational forms of chymotrypsin are confirmed.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)