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The haemocyanin of Limulus polyphemus is composed of a number (possibly 10-15) of polypeptides and is believed to be synthesised in cells called cyanoblasts. In vitro translation in the rabbit reticulocyte haemolysate system and in Xenopus oocytes, of mRNA isolated from cyanoblast-containing tissue, allowed the detection of several haemocyanin polypeptides amongst the products of translation. At least seven polypeptides with molecular weights in the range 68 000-71 000 were identified by an immunological method followed by electrophoretic characterisation on two-dimensional polyacrylamide gels. Comparison of the polypeptide patterns of authentic haemocyanin, reticulocyte lysate translation products and Xenopus oocyte translation products led to the conclusion that the polypeptides are unlikely to undergo significant post-translational modification or to possess cleavable signal sequences. It is proposed that release of haemocyanin into the haemolymph in vivo may involve bursting of the cyanoblasts.