Subunit Structure of Erythrocruorin from the Polychaete Tylorrhynchus heterochaetus

Abstract

Sodium dodecyl sulfate (SDS)-gel electrophoresis of erythrocruorin from the polychaete Tylorrhynchus heterochaetus revealed the presence of four subunits with molecular weights of 12, 000, 22, 000, 23, 500, and 54, 000 in a molar ratio of 6:1:2:3, respectively. The largest subunit dissociates into polypeptide chains of 13, 500 molecular weight in the presence of mercaptoethanol, whereas each of the other subunits consists of a single polypeptide chain. Hemochromogen determination gave a minimum molecular weight of 26, 500 per mol of heme group.
A model of the subunit structure of the erythrocruorin molecule is proposed, composed of 144 subunits (252 polypeptide chains) possessing 144 heme groups. The molecular weight of the erythrocruorin was calculated to be 3.636×10⁶