Purification and crystallization of haemoglobin from donkey (Equus asinus).
Haemoglobin acts as an important protein for oxygen carrier in all living beings. Purification of donkey haemoglobin was done using PEG 4000 as a separating medium. Crystallization was achieved using hanging drop vapor diffusion method using 2.8 M phosphate buffer, pH 6.8. Data collection was done using mar345 image plate detector system. The crystals grown under 2.8 M phosphate buffer are monoclinic with space group C2 and cell dimensions a=107.664 A, b=63.084 A, c=54.042 A, and beta=111.747 degrees.
Balasundaresan
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Department of Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai 600025, India.
Saraboji
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Ponnuswamy
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MN
D000818:Animals; D018360:Crystallography, X-Ray / Q000379:methods*; D018397:Equidae; D006454:Hemoglobins / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013329:Structure-Activity Relationship
D006454:Hemoglobins