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Mink Growth Hormone Structural–Functional Relationships: Effects of Renaturing and Storage Conditions

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Abstract

Fourier-transform infrared spectroscopy, in vitro bioassay and enzyme-linked immunoassay were used to study the structural-functional relationships of recombinant mink growth hormone (mGH), refolded and stored under different conditions. Porcine GH (pGH) was synthesized and used as an example. These two hormones, when refolded and stored the same way, had the same secondary structures, biological and immunological efficacy, and biological potency. Only the immunological potency differed, mGH being significantly less potent than pGH. Renaturation pH and storing frozen or at 4 °C in 5% glycerol did not affect either the secondary structure or the activity. However, freeze-drying raised the content of buried α-helices and lowered that of solvated α-helices and of unordered structures. These conformational changes were associated with a reduction of immunological and biological potency of mGH and of immunological potency of pGH. These findings provide original information on the secondary structure of mGH, and show that conformational changes induced by lyophilization adversely affect its activity.

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Abbreviations

Amide I′:

Amide I in 2H2O medium

FT-IR:

Fourier-transform infrared

GH:

Growth hormone

mGH:

Mink growth hormone

pGH:

Porcine growth hormone

GH-8-F:

GH refolded at pH 8.0, stored frozen

GH-8-L:

GH refolded at pH 8.0, stored lyophilized at 4 °C

GH-9-F:

GH refolded at pH 9.0, stored frozen

GH-9-G:

GH refolded at pH 9.0, stored at 4 °C, 5 % glycerol

GH-9-L:

GH refolded at pH 9.0, stored lyophilized at 4 °C

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Authors and Affiliations

  1. Department of Animal Pathology and Health, Biochemistry and Physiology Unit, Faculty of Veterinary Medicine, University of Milan, Via Celoria 10, 20133, Milan, Italy

    Vitaliano Borromeo & Camillo Secchi

  2. Department of Veterinary Pathology, Hygiene and Health, Biochemistry and Physiology Unit, University of Milan, Via Celoria 10, 20133, Milan, Italy

    Vitaliano Borromeo

  3. Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Vilnius, Lithuania

    Jolanta Sereikaite & Vladas-Algirdas Bumelis

  4. Institute of Biochemistry, Faculty of Sciences, Università Politecnica delle Marche, Ancona, Italy

    Andrea Scirè, Alessio Ausili & Fabio Tanfani

  5. Institute of Protein Biochemistry, CNR, Naples, Italy

    Sabato D’Auria

Authors
  1. Vitaliano Borromeo
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  2. Jolanta Sereikaite
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  3. Vladas-Algirdas Bumelis
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  4. Camillo Secchi
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Correspondence to Vitaliano Borromeo.

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Borromeo, V., Sereikaite, J., Bumelis, VA. et al. Mink Growth Hormone Structural–Functional Relationships: Effects of Renaturing and Storage Conditions. Protein J 27, 170–180 (2008). https://doi.org/10.1007/s10930-007-9120-1

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