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Functional role of arginine residues in glutamic acid decarboxylase from brain and bacteria

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Summary

The arginine-specific reagent phenylglyoxal rapidly inactives glutamic decarboxylase from both mouse brain andE. coli when preincubated with the enzyme at concentrations of 3 mM to 40 mM. The rate of inactivation follows pseudo-first-order kinetics and is dependent upon the concentration of phenylglyoxal. These and other data presented support the idea that arginine residues play a key role in the mechanism of action of glutamic decarboxylase.

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Authors and Affiliations

  1. Laboratory of Neurochemistry, Clinical Research Institute of Montreal, 110 Pine Avenue West, H2W 1R7, Montreal, Quebec, Canada

    G. Tunnicliff & T. T. Ngo

  2. Department of Medicine, University of Montreal, 110 Pine Avenue West, H2W 1R7, Montreal, Quebec, Canada

    G. Tunnicliff & T. T. Ngo

Authors
  1. G. Tunnicliff
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  2. T. T. Ngo
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Tunnicliff, G., Ngo, T.T. Functional role of arginine residues in glutamic acid decarboxylase from brain and bacteria. Experientia 34, 989–990 (1978). https://doi.org/10.1007/BF01915304

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  • DOI: https://doi.org/10.1007/BF01915304

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