Preparation and kinetic properties of a new form of chymotrypsin which is active at alkaline pH: α1 chymotrypsin

P. Valenzuela, M. L. Bender

Resultado de la investigación: Contribución a una revistaArtículo

11 Citas (Scopus)

Resumen

The preparation of a new stable and active form of chymotrypsin is described. The enzyme possesses the threonine 147 instead of alanine 149 as the NH2 terminal group of the C chain and has been called α1 chymotrypsin. The conformational transition that affects chymotrypsins at alkaline pH was investigated and compared with that of α- and δ chymotrypsins by studying the kinetic constants and their pH dependencies for the hydrolysis of various specific ester substrates. The k(cat) values obtained with α1 chymotrypsin are similar to those of α- and δ chymotrypsins. The K(m) values showed a progressive increase toward the alkaline pH region. The shape of the K(m) pH profiles closely resemble those of δ chymotrypsin and differ considerably from the behavior of α chymotrypsin. The results strongly implicate the participation of the alanine 149 amino group in the reversible inactivation of α chymotrypsin at high pH.

Idioma originalInglés
Páginas (desde-hasta)4909-4914
Número de páginas6
PublicaciónJournal of Biological Chemistry
Volumen248
N.º14
EstadoPublicada - 1973

Áreas temáticas de ASJC Scopus

  • Bioquímica
  • Medicina (todo)
  • Biología molecular
  • Biología celular

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