DETERMINATION OF THE INTRINSIC MICHAELIS CONSTANT OF IMMOBILIZED ALPHA-CHYMOTRYPSIN

Authors
Citation
S. Blais et R. Lortie, DETERMINATION OF THE INTRINSIC MICHAELIS CONSTANT OF IMMOBILIZED ALPHA-CHYMOTRYPSIN, The Journal of biological chemistry, 268(25), 1993, pp. 18637-18639
Citations number
11
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
268
Issue
25
Year of publication
1993
Pages
18637 - 18639
Database
ISI
SICI code
0021-9258(1993)268:25<18637:DOTIMC>2.0.ZU;2-A
Abstract
The Michaelis constant of alpha-chymotrypsin, immobilized on a glutara ldehyde-activated silicate support, for N-glutaryl-L-phenylalanine-p-n itroanilide was determined and was found to be identical with that of the enzyme in solution. The influence of intraparticular diffusion was taken into account by immobilizing different amounts of enzyme, thus changing the magnitude of diffusional constraints and extrapolating ap parent Michaelis constants, determined for each amount of immobilized enzyme, to zero diffusional constraints. The possible effect of the im mobilized enzyme distribution inside the porous matrix was investigate d through numerical simulations.