Properties of trout hemoglobin covalently bound to a solid matrix.
This paper reports the ligand binding properties of the major hemoglobin component from trout (Salmo irideus) covalently bound to a solid matrix (Sepharose or Sephadex). A comparison between the functional properties of this protein in solution and of the protein-matrix complex shows significant changes although the basic properties of the molecule are maintained on covalent binding to Sepharose (or Sephadex). Thus the Root effect, characteristic of Hb trout IV, is still present while the heme-heme interactions are, on the average, smaller in the matrix bound protein as compared to the soluble form. No differences in the O2 binding properties were observed when the protein was coupled to the resin, as the ligand bound or as the ligand free derivative. Although an unequivocal interpretation of the data is made difficult by the lack of information on the number and identity of the groups involved in the coupling, the main changes in the protein functional properties may be related to the chemical modifications "per se" more than to the immobilization imposed to the macromolecule by coupling to the matrix. Structural changes which mainly involve perturbation of the tertiary structure of the molecule may qualitatively rationalize the data.
D000818:Animals; D055598:Chemical Phenomena; D002621:Chemistry; D006454:Hemoglobins / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D010108:Oxyhemoglobins / Q000378:metabolism; D011487:Protein Conformation; D012487:Salmonidae / Q000097:blood*; D012685:Sepharose; D012995:Solubility; D013329:Structure-Activity Relationship; D014337:Trout / Q000097:blood*
D006454:Hemoglobins; D008024:Ligands; D010108:Oxyhemoglobins; D012685:Sepharose