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...
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Published in | Journal of enzyme inhibition and medicinal chemistry Vol. 19; no. 2; pp. 157 - 160 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
England
Taylor & Francis
01.04.2004
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Abstract | 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. |
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AbstractList | 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 = 300K. The Ki and enthalpy of binding for calcium (13.4, 13.1 mM and -14.3 kJ/mol), magnesium (18.6, 17.8mM 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. 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. |
Author | Umar Dahot, M. Moosavi-Movahedi, A.A. Saboury, A.A. |
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References | Saboury A.A. (CIT0012) 2003; 72 Mordasini T. (CIT0014) 2003; 278 Bernfeld P. (CIT0006) 1955; 1 Santos M.M. (CIT0003) 1996; 102 Saboury A.A. (CIT0010) 1997; 12 Saboury A.A. (CIT0008) 2002; 35 Sarraf N.S. (CIT0011) 2002; 17 CIT0002 CIT0013 CIT0005 Robyt J.F. (CIT0001) 1968 Whileley C.G. (CIT0004) 2000; 33 Dixon M. (CIT0007) 1953; 55 CIT0009 |
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SubjectTerms | beta-Amylase - antagonists & inhibitors Calcium - pharmacology Calorimetry - methods Cations, Divalent Inhibition Isothermal titration calorimetry Kinetics Magnesium - pharmacology Metal ions Spectrophotometry Zinc - pharmacology β-Amylase |
Title | Inhibition of β-Amylase Activity by Calcium, Magnesium and Zinc Ions Determined by Spectrophotometry and Isothermal Titration Calorimetry |
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