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Preparation and Kinetic Properties of a New Form of Chymotrypsin Which Is Active at Alkaline pH: agr1-Chymotrypsin

Pablo Valenzuela 1 and Myron L. Bender 2

From the 1 From the Laboratorio de Bioquimica, Departamento de Biologia Celular I.C.B., Universidad Catolica, Casilla 114-D, Santiago, Chile
2 From the Division of Biochemistry, Department of Chemistry, Northwestern University, Evanston, Illinois 60201

The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses threonine-147 instead of alanine-149 as the NH2-terminal group of the C chain and has been called agr1-chymotrypsin.

The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of agr- and dgr-chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The kgrcat values obtained with agr1-chymotrypsin are similar to those of agr- and dgr-chymotrypsins. The Km values showed a progressive increase toward the alkaline pH region. The shape of the Km-pH profiles closely resemble those of dgr-chymotrypsin and differ considerably from the behavior of agr-chymotrypsin. The results strongly implicate the participation of the alanine-149 amino group in the reversible inactivation of agr-chymotrypsin at high pH.

Submitted on January 18, 1973


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