Purification, crystallization and preliminary analysis of hemoglobin from rabbit (Oryctolagus cuniculus) |
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| Authors: | Sundaresan Sigamani Charles Packianathan Neelagandan Kamariah Ponnuswamy Mondikalipudur Nanjappa Gounder |
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| Institution: | Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai - 600 025, India. |
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| 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 3,350 as the precipitant at 18 degrees C. The crystals of rabbit Hb belongs to triclinic space group P1 with one molecule (alpha2beta2) in the asymmetric unit. |
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