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Physicochemical and functional properties of Pernereis cultrifera (Grübe) erythrocruorin

1977; Elsevier BV; Volume: 494; Issue: 1 Linguagem: Inglês

10.1016/0005-2795(77)90129-5

1878-1454

Emilia Chiancone, Franca Ascoli, Bruno Giardina, Paola Vecchini, Eraldo Antonini, Maria Teresa Musmeci, Renata Cinà, Michela Zagra, Vincenzo D'Amelio, Giacomo De Leo,

Mass Spectrometry Techniques and Applications

Perinereis erythrocruorin has the following physicochemical properties: So20,w = 55S, corresponding to a molecular weight around 2.7-10(6); minimum molecular weight (on the basis of the heme content) 23 700 +/- 500; isoelectric point 5.1; alpha-helix content approximately 40%. At alkaline pH values in the oxygenated form the 55-S molecules dissociate into subunits with a weight average sedimentation coefficient of 3S, corresponding to a molecular weight approximately 35 000. Deoxygenation of partially dissociated samples promotes association of the 3-S subunits into a 9S component. The functional properties of Perinereis erythrocruorin are characterized by a low cooperativity in oxygen binding (n 1/2 = 1.5) at neutral pH. Cooperativity increases reversibly towards both the acid and alkaline pH range, irrespective of changes in molecular weight. This finding, taken together with the ultracentrifuge results, suggests that a subunit may represent the functional unit of the protein. The pH dependence of the oxygen affinity can be accounted for in terms of a single oxygen linked group with a pK of 8.