Purification, crystallization and preliminary crystallographic study of low oxygen-affinity haemoglobin from cat (Felis silvestris catus) in two different crystal forms

Balasubramanian Moovarkumudalvan, Pon Sathya Moorthy, K. Neelagandan, M. N. Ponnuswamy

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Haemoglobin is a metalloprotein which plays a major role in the transportation of oxygen from the lungs to tissues and of carbon dioxide back to the lungs. The present work reports the preliminary crystallographic study of low oxygen-affinity haemoglobin from cat in different crystal forms. Cat blood was collected, purified by anion-exchange chromatography and crystallized in two different conditions by the hanging-drop vapour-diffusion method under unbuffered low-salt and buffered high-salt concentrations using PEG 3350 as a precipitant. Intensity data were collected using MAR345 and MAR345dtb image-plate detector systems. Cat haemoglobin crystallizes in monoclinic and orthorhombic crystal forms with one and two whole biological molecules (́2β2), respectively, in the asymmetric unit.

Original languageEnglish
Pages (from-to)313-316
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number3
DOIs
Publication statusPublished - 13 Mar 2009
Externally publishedYes

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cats
hemoglobin
Crystallization
purification
Purification
affinity
Hemoglobins
Cats
crystallization
Oxygen
lungs
Crystals
oxygen
Salts
Metalloproteins
salts
crystals
Lung
chromatography
Chromatography

Keywords

  • Haemoglobin
  • Low oxygen affinity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Structural Biology
  • Genetics
  • Condensed Matter Physics

Cite this

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AU - Neelagandan, K.

AU - Ponnuswamy, M. N.

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