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Citation: LI Wei-Guo, QI Chaob, LIU Li-Yana, ZHAO Da-Qinga. Enzymatic and Spectroscopic Studies on the Interaction of Lactate Dehydrogenase with DTPA and its Derivatives[J]. Chinese Journal of Applied Chemistry, ;2005, 22(11): 1172-1177. shu

Enzymatic and Spectroscopic Studies on the Interaction of Lactate Dehydrogenase with DTPA and its Derivatives

1.
a Key Laboratory of Rare Earth Chemistry and Physics, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun 130022;
2.
b College of Life Science, Central China Normal University, Wuhan

Corresponding author: LI Wei-Guo,
Received Date: 20 January 2005
Available Online: 8 May 2005
Fund Project: 国家自然科学基金重大项目(29890280) (29890280)

The enzymatic interactions between lactate dehydrogenase and diethylenetriamine pentaacetic acid(DTPA) and its derivatives bisdimethylamide-diethylenetriamine pentaacetic acid(DTPA-BDMA) and bisisonicotinyl-diethylenetriamine pentaacetic acid(DTPA-BIN) have been investigated.DTPA and its derivatives react as competitive inhibitors and inhibit the activity of lactate dehydrogenase,the inhibition constants are 3.37,7.41,8.52 μmol/L,respectively.The results from Ultraviolet-Visible difference spectroscopy indicate that after binding with lactate dehydrogenase molecule,the carboxyl groups of DTPA are embedded in an inner hydrophobic environment.DTPA and its derivatives could reduce the tryptophan fluorescence emission intensity of dehydrogenase and exhibit little effects on the tyrosine fluorescence intensity.
- diethylenetriamine pentaacetic acid,
- lactate dehydrogenase,
- enzymatic kinetics,
- UV difference spectroscopy,
- fluorescence spectroscopy
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