Primary structure of CHH/MIH/GIH-like peptides in sinus gland extracts from Penaeus vannamei

Peptides. 2000 Apr;21(4):477-84. doi: 10.1016/s0196-9781(00)00177-7.

Abstract

Peptides belonging to the CHH/MIH/GIH-family of crustacean hormones were isolated from acetic acid extracts of sinus glands isolated from eyestalks of the shrimp, Penaeus vannamei. The peptides were isolated by chromatography and molecular weights determined by MALDI mass spectrometry. Peptides in the range of 7-9 kDa and containing three disulfide bridges were selected for amino acid sequence analysis. Three peptides with the requisite properties were present in sufficient amounts for sequence analysis. Two peptides had unique sequences similar to CHH/MIH/GIH peptides from other crustaceans. A third peptide seemed to be a truncated form of one of the previous sequences.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Proteins
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Cyanogen Bromide
  • Endopeptidases
  • Eye / chemistry
  • Invertebrate Hormones / chemistry*
  • Invertebrate Hormones / isolation & purification
  • Molecular Sequence Data
  • Neuropeptides / chemistry*
  • Neuropeptides / isolation & purification
  • Penaeidae / chemistry*
  • Peptide Mapping
  • Sequence Analysis, Protein
  • Sequence Homology, Amino Acid
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Arthropod Proteins
  • CHH-like protein, shrimp
  • Invertebrate Hormones
  • Neuropeptides
  • molt-inhibiting hormone-like neuropeptide
  • Endopeptidases
  • Cyanogen Bromide