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Fig. 5. The structural model of native form of whale sperm myoglobin (1VXA) has been
colored red (polypeptide chain) and purple (ligands-heme and sulphate ion). The structural
polypeptide chain of horse myoglobin (1DWR) has been colored green and the ligands (heme
and sulphate ions) have been colored yellow. Both proteins can be fitted with the RMS = 0.01
Å (carbons alpha only), including that both molecules are structurally almost identical. The
amino acids sequences of both proteins are 94% identical. Despite the great structural simi-
larities only horse myoglobin, but not whale myoglobin, was adsorbed onto the column pre-
pared specifically for horse myoglobin (Fig. 4). The column was thus highly selective.
The detailed procedure was as follows. 100-mesh granules of a T6, C5
gel specific for adsorption of hemoglobin were prepared in 1 mL of 0.01 M
sodium phosphate pH 7.0, essentially as described for the above “growth
hormone column” (the hemoglobin concentration in the monomer solution
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