[Direct allosteric interaction of oxygen and bicarbonate: N-acetyl-alanyl-seryl-phenylalanine, N-terminal sequence of the beta-chains of the haemoglobins of Nil crocodile (Crocodylusniloticus) and Mississippi crocodile (Alligator mississippiensis) (author's transl)].
To elucidate the molecular mechanism of the direct allosteric exchange of oxygen and hydrogen carbonate in the hemoglobins of crocodiles, the N-terminal sequence of the beta-chains of the crocodiles of the Nile (Crocodylus niloticus) and of the Mississippi (Alligator mississippiensis) was studied. The N-terminal end of the peptide is blocked. By mass spectrometry the N-terminal sequences of both species were found to be N-acetyl-alanyl-seryl-phenylalanine. These data explain the absence of hemoglobinphosphate interaction, the data are in good agreement with the stereochemistry postulated for allosteric exchange of oxygen and hydrogen carbonate in crocodilian hemoglobins.
D000489:Alligators and Crocodiles / Q000097:blood*; D000595:Amino Acid Sequence; D000818:Animals; D001639:Bicarbonates / Q000494:pharmacology*; D006454:Hemoglobins / Q000378:metabolism*; D013058:Mass Spectrometry; D010108:Oxyhemoglobins / Q000378:metabolism*; D012104:Reptiles / Q000097:blood*; D013045:Species Specificity
D001639:Bicarbonates; D006454:Hemoglobins; D010108:Oxyhemoglobins
Direkte allosterische Wechselwirkung von Sauerstoff und Bicarbonat: N-Acetyl-Ala-Ser-Phe, die N-terminale Sequenz der beta-Ketten der Hämoglobine des Nikrokodils (Crocodylus niloticus) und des Mississippi-krokodils (Alligator mississippiensis).