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

• Published in: Peptides (New York, N.Y. : 1980) Vol. 21; no. 4; pp. 477 - 484
• Main Authors: Wang, Yajun J, Hayes, Timothy K, Holman, G.Mark, Chavez, Antonio R, Keeley, Larry L
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.04.2000
• Subjects: Amino Acid Sequence; Animals; Arthropod Proteins; Brackish; CHH; Chromatography, Gel; Chromatography, High Pressure Liquid; Crustacean neuropeptides; Cyanogen Bromide; Endopeptidases; Eye - chemistry; GIH family; Invertebrate Hormones - chemistry; Invertebrate Hormones - isolation & purification; Litopenaeus vannamei; Marine; MIH; Molecular Sequence Data; Neuropeptides - chemistry; Neuropeptides - isolation & purification; Penaeidae - chemistry; Peptide chemistry; Peptide Mapping; Sequence Analysis, Protein; Sequence Homology, Amino Acid; Shrimp hormones; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; CHH; Crustacean neuropeptides; Amino acid sequence; GIH family; Peptide chemistry; Shrimp hormones; MIH
• ISSN: 0196-9781; 1873-5169
• DOI: 10.1016/S0196-9781(00)00177-7

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.