Preliminary Crystallographic Study of Hemoglobin from Buffalo (Bubalus bubalis): A Low Oxygen Affinity Species.
Hemoglobin is a tetrameric, iron-containing metalloprotein, which plays a vital role in the transportation of oxygen from lungs to tissues and carbon dioxide back to lungs. Though good amount of work has already been done on hemoglobins, the scarcity of data on three dimensional structures pertaining to low oxygen affinity hemoglobins from mammalian species, motivated our group to work on this problem specifically. Herein, we report the preliminary crystallographic analysis of buffalo hemoglobin, which belongs to low oxygen affinity species. The buffalo blood was collected, purified by anion exchange chromatography and crystallized with PEG 3350 using 50mM phosphate buffer at pH 6.7 as a precipitant by hanging drop vapor diffusion method. Data collection was carried out using mar345dtb image plate detector system. Buffalo hemoglobin crystallizes in orthorhombic space group P2(1)2(1)2(1) with one whole biological molecule (alpha2beta2) in the asymmetric unit with cell dimensions a=63.064A, b=74.677A, c=110.224A.
Balasubramanian
Moovarkumudalvan
M
Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai - 600 025, India. mnpsy2004@yahoo.com.
Moorthy
Ponnuraj Sathya
PS
Neelagandan
Kamariah
K
Ponnuswamy
Mondikalipudur Nanjappa Gounder
MN
D000818:Animals; D002020:Buffaloes / Q000097:blood*; D002852:Chromatography, Ion Exchange; D018360:Crystallography, X-Ray; D006454:Hemoglobins / Q000737:chemistry*
D006454:Hemoglobins