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The erythrocruorin of eisenia foetida 1. properties and subunit structure


, : The erythrocruorin of eisenia foetida 1. properties and subunit structure. Biochimica et Biophysica Acta 704(3): 524-534

The erythrocruorin of E. foetida possesses a relative molecular mass, determined by sedimentation equilibrium, of (3.82 .+-. 0.05) 106. According to the Fe and heme contents, 0.218 .+-. 0.008% and 2.34 .+-. 0.02% by mass, respectively, it contains 144 hemes/molecule. The dimensions of the molecule observed by EM are 25.0 .times. 16.5 nm (diameter .times. height). SDS[sodium dodeayl sulfate]-polyacrylamide gel electrophoresis indicates that the erythrocruorin consists of 6 subunits (MW 14,900, 15,300, 17,200, 19,700, 31,600 and 40,000). O2 binding studies showed that E. foetida erythrocruorin has a high O2 affinity (P50 [50% saturation] = 2.8 Torr at pH 7.5), exhibits a slight Bohr effect and possesses a high cooperativity with the Hill coefficient h = 3.7-4.8. Treatment of the erythrocruorin either by freezing and thawing, aging or exposure to alkaline pH converts it irreversibily into a state of lower cooperativity with h = 2.0-2.6. A model of the subunit structure of the erythrocruorin is proposed which takes into account the physiochemical and O2-binding properties of the erythrocruorin and the subunits obtained upon its dissociation.

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PMID: 7115725


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