Inhibition of β-Amylase Activity by Calcium, Magnesium and Zinc Ions Determined by Spectrophotometry and Isothermal Titration Calorimetry

The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and isothermal titration calorimetric (ITC) methods. The binding of calcium, magnesium and zinc ion as inhibitors at the active site of barley beta amyla...

Full description

Saved in:
Bibliographic Details
Published inJournal of enzyme inhibition and medicinal chemistry Vol. 19; no. 2; pp. 157 - 160
Main Authors Umar Dahot, M., Saboury, A.A., Moosavi-Movahedi, A.A.
Format Journal Article
LanguageEnglish
Published England Taylor & Francis 01.04.2004
Subjects
beta-Amylase - antagonists & inhibitors
Calcium - pharmacology
Calorimetry - methods
Cations, Divalent
Inhibition
Isothermal titration calorimetry
Kinetics
Magnesium - pharmacology
Metal ions
Spectrophotometry
Zinc - pharmacology
β-Amylase
Online AccessGet full text

Cover

More Information
Summary:The inhibition effect of metal ions on beta amylase activity was studied. The inhibitor-binding constant (Ki) was determined by spectrophotometric and isothermal titration calorimetric (ITC) methods. The binding of calcium, magnesium and zinc ion as inhibitors at the active site of barley beta amylase was studied at pH=4.8 (sodium acetate 16 mM) and T=300 K. The Ki and enthalpy of binding for calcium (13.4, 13.1 mM and -14.3 kJ/mol), magnesium (18.6, 17.8 mM and -17.7 kJ/mol) and zinc (17.5, 17.7 mM and -20.0 kJ/mol) were found by spectrophotometric and ITC methods respectively.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1475-6366
1475-6374
DOI:10.1080/14756360310001650255