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January 24, 2010 | History

Kinetic studies of novel reversible and mechanism-based inhibitors of orotidine monophosphate decarboxylase and serine proteases 1 edition

Kinetic studies of novel reversible and mechanism-based inhibitors of ...
Ewa Poduch

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Kinetic studies of novel reversible and mechanism-based inhibitors of orotidine monophosphate decarboxylase and serine proteases.

Published 2006 .
Written in English.

About the Book

Enzyme inhibitors are the subjects of intense investigation due to their abilities to modulate enzyme activities. The profiles of novel inhibitors of orotidine monophosphate decarboxylase (ODCase) and serine proteases are described here. Inhibitors of ODCase designed using the principles of bioisosteric replacement were characterized using a new Isothermal Titration Calorimetry (ITC)-based method. Various modes of inhibition were observed ranging from a classical reversible inhibition through a mechanism-based to an irreversible enzyme inactivation. For the first time the covalent species formation was observed with ODCase. Inhibitory characteristics of selected compounds from two libraries of fluoropeptidomimetics and "His-block" inhibitors were evaluated against chymotrypsin, a serine protease. Both types of inhibitors showed concentration- and time-dependent inhibition. The dissociation constant, K I and the maximal rate of inactivation (kinact ) were derived for each inhibitor tested. The determination of kinetic profiles of novel inhibitors is an important part of the drug development process.

Edition Notes

Source: Masters Abstracts International, Volume: 44-06, page: 2776.

Thesis (M.Sc.)--University of Toronto, 2006.

Electronic version licensed for access by U. of T. users.

ROBARTS MICROTEXT copy on microfiche.

The Physical Object

Pagination
123 leaves.
Number of pages
123

ID Numbers

Open Library
OL19215288M
ISBN 13
9780494161968

History

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January 24, 2010 Edited by WorkBot add more information to works
December 11, 2009 Created by WorkBot add works page