Abstract
Hemoglobin from the cobra snake, Naja naja naja, was isolated and its chains separated on a CM-cellulose column. The separation profile revealed an α and two β chains having the molar proportions of [α]2,[β 1]1,[β 2]1. The N-terminal amino acid sequence of the intact chains and of the CNBr peptides were carried out. Theβ 2 chain was found to be heterogeneous comprising a minor component amounting to 11%. This later showed changes at two positions 9 and 14 in the first 30 residues sequenced.
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References
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Naqvi, S., Nadvi, I.N. & Zaidi, Z.H. Partial sequence of hemoglobin from cobra (Naja naja naja). Biosci Rep 7, 813–819 (1987). https://doi.org/10.1007/BF01116755
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DOI: https://doi.org/10.1007/BF01116755