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The primary structure of sperm whale hemoglobin (Physeter catodon, cetacea)


Biological Chemistry Hoppe-Seyler 367(4): 355-361
The primary structure of sperm whale hemoglobin (Physeter catodon, cetacea)
The complete primary structure of the two major hemoglobin components of sperm whale (Physeter catodon) is presented. The major components A and B account for 55% and 40% respectively whereas the minor component constitutes for 5% of the total hemoglobin. The globin chains were separated on CM-Cellulose in 8M urea buffer. The sequence was determined by automatic Edman degradation of tryptic and hydrolytic peptides in a liquid phase sequencer. Alignment of the sequence with human hemoglobin shows 22 exchanges each for the .alpha.I and .alpha.II and 21 exchanges for the .beta.I and .beta.II chains. Within the two .beta.-chains three differences have been located, .beta.NA2 His/Gln, .beta.A2 Gly/Ala and .beta.A8 Leu/Val. The two .alpha.-chains are characterized by heterogeneities at position .alpha.A8 Val/Lle or Ala/Ile (ratio of the phenylthiohydantoin derivatives of the amino acids 1:1) and .alpha.AB1 Asn/Ser (ratio of the phenylthiohydantoin derivatives of the amino acids 6:4). The role of these exchanges in modulating oxygen affinity is discussed.


Accession: 006740993

PMID: 3718676

DOI: 10.1515/bchm3.1986.367.1.355



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