Cuticular proteins from the horseshoe crab, Limulus polyphemus

Proteins were purified from the carapace cuticle of a juvenile horseshoe crab, Limulus polyphemus, and several of them were characterized by amino acid sequence determination. The proteins are small (7-16 kDa) and their isoelectric points range from 6.5 to 9.2. They have high contents of tyrosine, ranging from 13.5 to 35.4%. Some of the proteins show sequence similarity to cuticular proteins from other arthropod groups, with the most pronounced similarity to proteins from the cuticle of the spider Araneus diadematus. Two proteins show sequence similarity to a hexamerin storage protein from Blaberus discoidalis.