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The Study of the Metal-Binding Region in Human Growth Hormone Using Immobilized Metal Ion Affinity Gel-Electrophoresis

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Abstract

The zinc(II)-binding affinities of recombinant human growth hormone and two its mutants, 14–33 and 14–95, were studied using Immobilized Metal Ion Affinity Gel-electrophoresis (IMAG). The mutant hormones, composed of polypeptide chain segments of the human and porcine growth hormones, lacked His18, which may be crucial for binding of the intact hormone to the transition metal ions. The mutations did not affect the affinity of human growth hormone to immobilized zinc ions; the structural analysis implied that the human growth hormone contains two IDA–Zn(II) potential sorption sites formed by amino acid residues His21, Asp171, and Glu174 and/or His18 and Glu174.

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Authors and Affiliations

  1. Bioengineering Center, Russian Academy of Sciences, pr. 60-letya Oktyabrya 7/1, Moscow, 117312, Russia

    M. V. Anisimova, K. G. Skryabin & V. P. Varlamov

  2. Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP-7, Moscow, 117871, Russia

    A. A. Shulga, I. V. Levichkin & M. P. Kirpichnikov

  3. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Moscow, 117333, Russia

    K. M. Polyakov

  4. Université de Technologie de Compiégne, BP 649/60206, Compiégne Cedex, France

    M. A. Vijayalakshmi

Authors
  1. M. V. Anisimova
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  2. A. A. Shulga
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  3. I. V. Levichkin
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  4. M. P. Kirpichnikov
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  5. K. M. Polyakov
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  6. K. G. Skryabin
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  7. M. A. Vijayalakshmi
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  8. V. P. Varlamov
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Anisimova, M.V., Shulga, A.A., Levichkin, I.V. et al. The Study of the Metal-Binding Region in Human Growth Hormone Using Immobilized Metal Ion Affinity Gel-Electrophoresis. Russian Journal of Bioorganic Chemistry 27, 23–26 (2001). https://doi.org/10.1023/A:1009522917352

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  • DOI: https://doi.org/10.1023/A:1009522917352

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