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Immobilized apo‐myoglobin, a new stable reagent for measuring rates of heme dissociation from hemoglobin
Author(s) -
Gattoni Maurizio,
Boffi Alberto,
Chiancone Emilia
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00190-2
Subject(s) - myoglobin , heme , chemistry , hemeprotein , hemoglobin , globin , sepharose , cofactor , denaturation (fissile materials) , biochemistry , enzyme , nuclear chemistry
Apo‐myoglobin covalently linked on CNBr‐activated Sepharose 4B is proposed as a new heme acceptor for investigating the heme transfer reaction from hemoproteins. Immobilized apo‐myoglobin has the desirable properties of an ideal heme acceptor in that it is characterized by a high affinity for ferric heme, a high stability towards denaturation even at physiological temperatures and can be lyophilized for long‐term storage. The study of heme release from myoglobin at pH 5.0 and 37°C indicates that heme affinity is increased at least 10‐fold relative to the soluble protein. Experiments with human hemoglobin allowed the estimation of the heme release rates from both α and β chains and brought out the greater temperature sensitivity of the α chain heme‐globin linkage.