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

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

Volume: 15 Issue: 3

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

Affiliation:

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

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.

Cite this article as:

Gounder Ponnuswamy Nanjappa Mondikalipudur, Sundaresan Sigamani, Charles Packianathan and Neelagandan Kamariah, Purification, Crystallization and Preliminary Analysis of Hemoglobin from Rabbit (Oryctolagus cuniculus), Protein & Peptide Letters 2008; 15 (3) . https://dx.doi.org/10.2174/092986608783744144

DOI https://dx.doi.org/10.2174/092986608783744144	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305