Protein & Peptide Letters

Author(s): Elmar Jaenicke and Bruno Pairet

DOI: 10.2174/092986609787847983

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Crystallization of the Altitude Adapted Hemoglobin of Guinea Pig

Page: [444 - 446] Pages: 3

  • * (Excluding Mailing and Handling)

Abstract

Hemoglobin is the versatile oxygen carrier in the blood of vertebrates and a key factor for adaptation to live in high altitudes. Several structural changes are known to account for increased oxygen affinity in hemoglobin of altitude adapted animals such as llama and barheaded goose. Guinea pigs are adapted to live in high altitudes in the Andes and consequently their hemoglobin has an increased oxygen affinity. However, the structural changes responsible for the adaptation of guinea pig hemoglobin are unknown. Here we report the crystallization of guinea pig hemoglobin in the presence of 2.6 M ammonium sulfate and a preliminary analysis of the crystals. Crystals diffract up to a resolution of 2.0 Å. They are orthorhombic with space group C 2 2 21 and cell dimensions a = 84.08 Å, b = 90.21 Å and c = 83.44 Å.

Keywords: Altitude, adaptation, hemoglobin, guinea pig, Cavia porcellus