Journal of Thermal Analysis and Calorimetry
Volume/Issue:
Volume 77: Issue 3
Microcalorimetric studies on the non-competitive inhibition of bovine liver arginase
Authors:
X.-Y Xie Yangtze University Jingzhou College of Chemistry and Environment Engineering 434104 Hubei People's Republic of China E-mail 434104 Hubei People's Republic of China E-mail

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C.-X. Wang Wuhan University Wuhan College of Chemistry and Molecular Science 430072 Hubei People's Republic of China 430072 Hubei People's Republic of China

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Z.-Y. Wang Wuhan University Wuhan College of Chemistry and Molecular Science 430072 Hubei People's Republic of China 430072 Hubei People's Republic of China

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Pages:
1005–1012
Online Publication Date:
03 Jan 2005
Publication Date:
01 Sep 2004
Article Category:
Research Article
DOI:
https://doi.org/10.1023/b:jtan.0000041676.52420.c0
Keywords:
thermokinetics; bovine liver arginase; L-arginine; sodium fluoride; non-competitive inhibition
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Abstract  

Two methods, e.g. initial rate method and thermokinetic reduced extent method were presented for studies on non-competitive inhibition. Arginase-catalyzed the hydrolysis of L-arginine toL-ornithine and urea and the inhibition of this reaction by sodium fluoride were studied in the absence and presence of exogenous of Mn2+at 37C in 40 mM sodium barbiturate-hydrochloric acid buffer solution (pH 7.4). Both methods were successively used to determine the values of K1. The advances and disadvantages of each method were compared in this paper. Exogenous Mn2+ could result in more sensitivity of arginase to F-1. Since the inhibition of arginase by F-1 depends on the pH values of the reaction system and behave as a non-competitive inhibition, it probably due to its small volume and high electronic density allow it access to the activity site of the enzyme and replaces of -OH2 (or -OH) as the bridge ligand with Mn(II, II) cluster. However, further studies are necessary to determine the modes of interaction of F-1 with bovine liver arginase.

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Cover Journal of Thermal Analysis and Calorimetry
Journal of Thermal Analysis and Calorimetry
Print ISSN:
1388-6150
Online ISSN:
1572-8943

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Journal of Thermal Analysis and Calorimetry
Language English
Size A4
Year of
Foundation		 1969
Volumes
per Year		 1
Issues
per Year		 24
Founder Akadémiai Kiadó
Founder's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
Publisher Akadémiai Kiadó
Springer Nature Switzerland AG
Publisher's
Address		 H-1117 Budapest, Hungary 1516 Budapest, PO Box 245.
CH-6330 Cham, Switzerland Gewerbestrasse 11.
Responsible
Publisher		 Chief Executive Officer, Akadémiai Kiadó
ISSN 1388-6150 (Print)
ISSN 1588-2926 (Online)

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