The oxygen carrier hemocyanin occurs in the blood of Scutigera coleoptrata, a uniramous arthropod, as well as the crustaceans and chelicerates. The native polymer appears to be composed ofsubstructures having the same size and electron-dense image as those of other arthropod hemocyanins but assembled into a unique multiple and arranged in a unique configuration. The simplest explanation of these fridings is that the arthropod hemocyanins have a common origin, exemplifying a derived (as opposed to primitive) character shared by each of the three living groups.In contrast to the hemoglobins (Hbs), the hemocyanins (Hcs) are regarded as coherent in taxonomic distribution. They are found in only two groups: the molluscs, in three of the four classes examined, and the arthropods, in the crustaceans and chelicerates. Also unlike the Hbs, the Hcs are always widespread in a particular taxon. Therefore, the report by Rajulu (1) of a Hc-like substance in a single order of uniramous arthropods, the scutigeromorph centipedes, is somewhat surprising. All but a few of the Uniramia lack an 02 carrier in the blood, the exceptions containing Hb rather than Hc. The brief report (1) was based on high levels of blood Cu and N, the blue color of the blood, and its absorption peak at 340 nm, all of which resemble features of the chelicerates. He did not, however, present the decisive evidence-namely, reversible 02 binding. Later, when the amino acid composition of this protein proved to differ from that of a crustacean Hc, he identified it with less certainty (2). Not unexpectedly, his inference is treated tentatively in a recent volume on centipede biology (3). Moreover, the possibility ofHc in the Uniramia appears to be either unknown to or dismissed by proponents of various points of view in the current debate on arthropod phylogeny (4,5).Our findings show that the common house centipede Scutigera coleoptrata (Linnaeus) does contain a Hc that resembles the crustacean and chelicerate Hcs in fundamental structural features but differs in superficial respects. The molecule is of both structural and phylogenetic interest.
METHODS AND MATERIALSBlood, which does not clot, was withdrawn into a glass capillary from the pericardial cavity. With the exception of the samples used for electron microscopy, the blood was of necessity frozen and stored until the volume sufficient for a particular measurement accumulated.Activities of the inorganic ions in the blood were measured with ion-selective electrodes (6). Absorption of the native blood (in physiological saline) and the Hc subunits (in 10 mM EDTA at pH 8.95) was examined with a Beckman recording spectrophotometer. 02 binding was determined by the cell respiration method (6), using a miniaturized respirometer that accepts samples as small as 300 1ul.The Hc was purified on a 1 x 20 cm column of Sephacryl S-300 equilibrated with Tris buffer (0.1 ionic strength, pH 7.65) containing 50 mM MgCl2 (buffer A). Most of the Hc eluted in the void volume.Whole blood was electrophoresed on poly...