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.
Ditzel
Nicholas
N
Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, DK-5230 Odense M, Denmark.
Andersen
Svend Olav
SO
Højrup
Peter
P
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006737:Horseshoe Crabs / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D019476:Insect Proteins / Q000737:chemistry / Q000302:isolation & purification; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D013112:Spiders / Q000737:chemistry; D014443:Tyrosine / Q000737:chemistry
D019476:Insect Proteins; D011506:Proteins; C047663:cuticle proteins, insects; D014443:Tyrosine