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Glutamate Dehydrogenase Self-Assembly. An Application of the Light Scattering Temperature-Jump Technique to the Study of Protein Aggregation

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Chemical Relaxation in Molecular Biology

Part of the book series: Molecular Biology Biochemistry and Biophysics ((MOLECULAR,volume 24))

Abstract

Glutamate dehydrogenase catalyzes the reversible oxidative deamination of L-glutamate to α-ketoglutarate and ammonia with pyridine nucleotides as coenzyme

The above reaction plays a key role in linking nitrogen metabolism to the tricarboxylic acid cycle (Fig. 1).

Role of glutamate dehydrogenase (1) in cellular metabolism. Circles: points of feedback control. (From. STADTMAN, 1966)

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Authors
  1. D. Thusius
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Editors and Affiliations

  1. Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, Israel

    Israel Pecht

  2. Department of Medical Biophysics, Karolinska Institutet, S-10401, Stockholm 60, Sweden

    Rudolf Rigler

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Thusius, D. (1977). Glutamate Dehydrogenase Self-Assembly. An Application of the Light Scattering Temperature-Jump Technique to the Study of Protein Aggregation. In: Pecht, I., Rigler, R. (eds) Chemical Relaxation in Molecular Biology. Molecular Biology Biochemistry and Biophysics, vol 24. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-81117-3_10

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  • DOI: https://doi.org/10.1007/978-3-642-81117-3_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-81119-7

  • Online ISBN: 978-3-642-81117-3

  • eBook Packages: Springer Book Archive

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