Antagonistic effect of urea on oxygenation-linked binding of ATP in an elasmobranch hemoglobin.

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 Sci

journal_title

Life sciences

authors

Weber RE,Wells RM,Tougaard S

doi

10.1016/0024-3205(83)90105-4

subject

Has Abstract

pub_date

1983-05-02 00:00:00

pages

2157-61

issue

18

eissn

0024-3205

issn

1879-0631

pii

0024-3205(83)90105-4

journal_volume

32

pub_type

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