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Protein & Peptide Letters

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ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Purification, Crystallization and Preliminary Analysis of Hemoglobin from Rabbit (Oryctolagus cuniculus)

Author(s): Mondikalipudur Nanjappa Gounder Ponnuswamy, Sigamani Sundaresan, Packianathan Charles and Kamariah Neelagandan

Volume 15, Issue 3, 2008

Page: [318 - 319] Pages: 2

DOI: 10.2174/092986608783744144

Price: $65

Abstract

Hemoglobin (Hb) is a tetrameric protein, which contains four heme prosthetic groups, and each one is associated with a polypeptide chain. Herein, we report the rabbit hemoglobin which has intrinsically high oxygen affinity and possess highest sequence identity with human hemoglobin. The purified hemoglobin has been tried to crystallize in different crystallization conditions owing to its formation of various crystal systems. The rabbit Hb crystals were grown using PEG 3350 as the precipitant at 18° C. The crystals of rabbit Hb belongs to triclinic space group P1 with one molecule (α2β2) in the asymmetric unit.

Keywords: Hemoglobin, crystallization, unbuffered, oxygen affinity, space group, asymmetric unit

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