دورية أكاديمية

Methods to measure the kinetics of protease inhibition by serpins.

التفاصيل البيبلوغرافية
العنوان: Methods to measure the kinetics of protease inhibition by serpins.
المؤلفون: Horvath AJ; Australian Centre for Blood Diseases, Monash University, Melbourne, Victoria, Australia., Lu BG, Pike RN, Bottomley SP
المصدر: Methods in enzymology [Methods Enzymol] 2011; Vol. 501, pp. 223-35.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Academic Press Country of Publication: United States NLM ID: 0212271 Publication Model: Print Cited Medium: Internet ISSN: 1557-7988 (Electronic) Linking ISSN: 00766879 NLM ISO Abbreviation: Methods Enzymol Subsets: MEDLINE
أسماء مطبوعة: Original Publication: New York, Academic Press.
مواضيع طبية MeSH: Biological Assay*, Biochemistry/*methods , Serine Proteases/*metabolism , Serpins/*metabolism, Animals ; Binding Sites ; Chickens ; Dose-Response Relationship, Drug ; Humans ; Kinetics ; Protein Binding/drug effects ; Protein Interaction Domains and Motifs/drug effects ; Protein Structure, Secondary/drug effects ; Serine Proteases/chemistry ; Serpins/chemistry ; Serpins/pharmacology ; Spectrometry, Fluorescence
مستخلص: The serpin molecule has evolved an unusual mechanism of inhibition, involving an exposed reactive center loop (RCL) and conformational change to covalently trap a target protease. Successful inhibition of the protease is dependent on the rate of serpin-protease association and the efficiency with which the RCL inserts into β-sheet A, translocating the covalently bound protease and thereby completing the inhibition process. This chapter describes the kinetic methods used for determining the rate of protease inhibition (k(a)) and the stoichiometry of inhibition. These kinetic variables provide a means to examine different serpin-protease pairings, assess the effects of mutations within a serpin on protease inhibition, and determine the physiologically cognate protease of a serpin.
(Copyright © 2011 Elsevier Inc. All rights reserved.)
المشرفين على المادة: 0 (Serpins)
EC 3.4.- (Serine Proteases)
تواريخ الأحداث: Date Created: 20111115 Date Completed: 20120315 Latest Revision: 20111114
رمز التحديث: 20231215
DOI: 10.1016/B978-0-12-385950-1.00011-0
PMID: 22078537
قاعدة البيانات: MEDLINE
الوصف
تدمد:1557-7988
DOI:10.1016/B978-0-12-385950-1.00011-0