The hyperglycemic neuropeptide of the terrestrial isopod, Porcellio dilatatus. I. Isolation and characterization.
From isolated sinus glands of Porcellio dilatatus, a hyperglycemic neuropeptide (CHH) was purified by means of a single, two-step purification procedure which consisted of gel chromatography on Sephadex G-50, followed by high-performance liquid chromatography. The 5800- to 6100-Da peptide contains 50-52 amino acids residues. The amino acid composition is (Pro, Ile)1; His1-2; (Thr, Ser, Gly, Met, Tyr)2; (Val, Phe, Lys)3; (Ala, 1/2Cys, Leu, Arg)4; Glx5; Asx7; Trp, n.d. The amino acid composition differs from that of two decapod CHHs analyzed thus far. The N-terminus is blocked. The neuropeptide exhibits little or no interspecific hyperglycemic effect in the brachyuran, Uca pugilator, and its cross-reactivity and potency in the RIA for Carcinus-CHH is very low.
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D060829:Arthropod Proteins; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D003429:Cross Reactions; D003445:Crustacea / Q000502:physiology*; D004589:Electrophoresis, Disc; D007447:Invertebrate Hormones; D009419:Nerve Tissue Proteins / Q000032:analysis* / Q000302:isolation & purification; D011506:Proteins / Q000378:metabolism
D000596:Amino Acids; D060829:Arthropod Proteins; D007447:Invertebrate Hormones; D009419:Nerve Tissue Proteins; D011506:Proteins; C015947:hyperglycemic hormone, crustacean