Identification of One Tachykinin- and Two Kinin-Related Peptides in the Brain of the White Shrimp,Penaeus vannamei
Autor: | Geoffrey M. Coast, Bart Devreese, Jorgen Calderon, Anja Cerstiaens, Dirk Veelaert, Jozef Van Beeumen, Liliane Schoofs, Arnold De Loof, Julie Nieto, Rita Derua, Etienne Waelkens |
---|---|
Rok vydání: | 1998 |
Předmět: |
medicine.medical_specialty
animal structures Biophysics Cockroaches Kinins Biochemistry Penaeidae Tachykinins biology.animal Internal medicine medicine Animals Bioassay Penaeus Diuretics Molecular Biology Brain Chemistry Antiserum Cockroach Sequence Homology Amino Acid Edman degradation biology Research Support Non-U.S. Gov't Neuropeptides fungi Brain Hindgut Cell Biology Kinin biology.organism_classification Shrimp Endocrinology Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Sequence Analysis Autacoids Muscle Contraction |
Zdroj: | Biochemical and Biophysical Research Communications. 248:406-411 |
ISSN: | 0006-291X |
DOI: | 10.1006/bbrc.1998.8964 |
Popis: | This paper reports the purification of three myotropic neuropeptides from the white shrimp Penaeus vannamei. The central nervous systems of 3500 shrimps were extracted in an acidified solvent, after which four to five HPLC column systems were used to obtain pure peptides. A cockroach hindgut muscle contraction bioassay was used to monitor all collected fractions. The pure peptides were submitted to Edman degradation based automated microsequencing. Mass spectrometry and chemical synthesis confirmed the sequences. Ala-Pro-Ser-Gly-Phe-Leu-Gly-Met-Arg-NH2 (Pev-tachykinin, 934.1 Da) belongs to the tachykinin family with identified members in all vertebrate classes and some invertebrate classes: arthropods, annelids and molluscs. A very specific Pev-tachykinin antiserum was developed, which labels 4 neurosecretory cells in the brain. Ala-Ser-Phe-Ser-Pro-Trp-Gly-NH2 (Pev-kinin 1, 749.8 Da) and Asp-Phe-Ser-Ala-Trp-Ala-NH2 (Pev-kinin 2, 694.7 Da) are the first crustacean kinins. Pev-kinin 2 is the first kinin with a Trp-Ala-NH2 instead of a kinin-typical Trp-Gly-NH2 carboxyterminus. ispartof: Biochemical and Biophysical Research Communications vol:248 issue:2 pages:406-411 ispartof: location:United States status: published |
Databáze: | OpenAIRE |
Externí odkaz: |
Pro tento záznam nejsou dostupné žádné jednotky.