Abstract:
:The O2 affinity of "stripped" (cofactor-free) hemoglobin (Hb) of the elasmobranch, Squalus acanthias is decreased by ATP, the main erythrocytic phosphate cofactor but increased by urea at physiological concentration. When both compounds are present, as in life, urea decreases the ATP sensitivity, indicating that previous Hb oxygenation studies in the absence of urea overestimate the modulator role of phosphate cofactors in sharks. Whereas ATP decreases the O2 association equilibrium constant of the deoxygenated pigment, urea raises those of both the deoxy and the oxygenated states. Possible mechanisms for the urea-protein interactions i.e. binding at carboxy-termini or carbamylation of amino-termini of the protein chains, are discussed.
journal_name
Life Scijournal_title
Life sciencesauthors
Weber RE,Wells RM,Tougaard Sdoi
10.1016/0024-3205(83)90105-4subject
Has Abstractpub_date
1983-05-02 00:00:00pages
2157-61issue
18eissn
0024-3205issn
1879-0631pii
0024-3205(83)90105-4journal_volume
32pub_type
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