Evidence for a conformational polymorphism of invertebrate neurohormones. D-amino acid residue in crustacean hyperglycemic peptides.
Several large peptidic neurohormones have been isolated in crustaceans. In lobster and other related species, each of these neurohormones, and particularly the crustacean hyperglycemic hormone, occurs as two isoforms having the same peptidic sequence and molecular mass. We report here that these isoforms differ by the configuration of a single amino acid residue. The third residue (Phe3) of the lobster hyperglycemic hormones is in either the L- or D-configuration. In addition, we have shown that the biological activity of the two isoforms differs when considering the kinetics of their hyperglycemic effect.
Laboratoire de Biochimie et Physiologie du Développement, URA CNRS 686, Ecole Normale Supérieure, Paris, France.
D
D
Soyez
F
F
Van Herp
J
J
Rossier
J P
JP
Le Caer
C P
CP
Tensen
R
R
Lafont
D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins; D007447:Invertebrate Hormones / Q000737:chemistry* / Q000302:isolation & purification; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008121:Nephropidae / Q000737:chemistry*; D009419:Nerve Tissue Proteins / Q000737:chemistry* / Q000302:isolation & purification; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D012627:Sebaceous Glands / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D060829:Arthropod Proteins; D007447:Invertebrate Hormones; D009419:Nerve Tissue Proteins; D009842:Oligopeptides; D010446:Peptide Fragments; C015947:hyperglycemic hormone, crustacean