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Microcalorimetry investigation of synthetic hemoprotein (albumin‐heme)
Author(s) -
Huang Yubin,
Komatsu Teruyuki,
Tsuchida Eishun
Publication year - 2003
Publication title -
polymers for advanced technologies
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.61
H-Index - 90
eISSN - 1099-1581
pISSN - 1042-7147
DOI - 10.1002/pat.418
Subject(s) - heme , hemeprotein , isothermal titration calorimetry , isothermal microcalorimetry , chemistry , hemoglobin , human serum albumin , albumin , serum albumin , biochemistry , enthalpy , thermodynamics , physics , enzyme
Recombinant human serum albumin (rHSA) incorporating the iron(II) complex of the tetraphenylporphyrin derivative (FepivP or FecycP) is a synthetic O 2 ‐carrying hemoprotein [albumin‐heme (rHSA‐FepivP or rHSA‐FecycP)], which acts as a red blood cell substitute. The association and dissociation behavior of FepivP and FecycP with rHSA has been initially investigated by isothermal titration calorimetry. A strong heat release appeared after the injection of albumin‐heme into a large molar excess of rHSA. This exothermic enthalpy change was due to the transference of hemes to the other free albumins. The difference in the heme binding affinity to rHSA can be manifested in the enthalpy term. Copyright © 2003 John Wiley & Sons, Ltd.