The structure of Artemia sp. haemoglobin. Cleavage of the native molecules into functional units by limited subtilisin digestion.
Limited subtilisin digestion of the high-Mr haemoglobin of the crustacean Artemia sp. results in a series of fragments that are multiples of Mr 16000. Properties such as amino acid composition, iron content, absorption and c.d. spectra of the 16000-Mr functional units strongly resemble those of the intact haemoglobin molecules. The 16000-Mr functional units can bind O2 in a non-co-operative way. They thus represent the structural units from which the globin chains are built up.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001156:Artemia / Q000032:analysis*; D002850:Chromatography, Gel; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000378:metabolism; D007501:Iron / Q000032:analysis; D010100:Oxygen / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D011506:Proteins / Q000032:analysis; D013381:Subtilisins
D000596:Amino Acids; D006454:Hemoglobins; D010446:Peptide Fragments; D011506:Proteins; D007501:Iron; D013381:Subtilisins; D010100:Oxygen