Characterization of endorphins from the pituitary of the spiny dogfish Squalus acanthias |
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| Authors: | R G Lorenz A N Tyler K F Faull G Makk J D Barchas C J Evans |
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| Affiliation: | 1. Department of Physiology, Uskudar University Faculty of Medicine, Istanbul, Turkey;2. The Franciszek Górski Institute of Plant Physiology, Polish Academy of Sciences, Niezapominajek 21, Kraków, 30–239, Poland;3. Institute of Nuclear Physics Polish Academy of Science, 31342 Krakow, Poland;4. Department of Biophysics, Adnan Menderes University Medical Faculty, Aydin, Turkey;5. Department of Biophysics, Cerrahpaşa Faculty of Medicine, Istanbul University-Cerrahpaşa, Istanbul, Turkey;1. Center for Advancing Materials Performance from the Nanoscale (CAMP-Nano), State Key Laboratory for Mechanical Behavior of Materials, Xi''an Jiaotong University, Xi''an 710049, China;2. CAS Key Laboratory of Nuclear Materials and Safety Assessment, Institute of Metal Research, Chinese Academy of Sciences, Shenyang 110016, China;3. Shi-changxu Innovation Center for Advanced Materials, Institute of Metal Research, ChineseAcademy of Sciences, Shenyang 110016,China;1. Department of Biological Sciences, University of Manitoba, Winnipeg, MB R3T 0A8, Canada;2. Laboratory of Physiology, Atmosphere and Ocean Research Institute, University of Tokyo, Kashiwa, Chiba, Japan |
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| Abstract: | Opioid-like immunoreactive material was extracted from the pituitary and brain of the Spiny Dogfish Shark Squalus acanthias. The immunoreactive material in the pituitary extracts was purified to apparent homogeneity by reverse phase high performance liquid chromatography and subsequently characterized by amino acid analysis, Edman degradation and fast atom bombardment mass spectrometry. The largest opioid-like peptide isolated contained 30 amino acids and showed 80 percent homology with salmon endorphin-II but less than 50 percent homology with human beta-endorphin. Three structural variants of this molecule were also characterized. These variants were shown to be shorter N-terminal fragments, two of which corresponded to cleavage products at the single basic residues arginine and lysine. Cleavage at a single lysine residue has not been reported for posttranslational processing of beta-endorphin in mammals and could represent a modification seen only in lower vertebrates. The remaining fragment corresponded to a loss of 3 residues from the C-terminus of the parent molecule. No alpha-N-acetylated peptides were detected. These results provide the first unequivocal confirmation of beta-endorphin in an elasmobranch and provide evidence of novel N-terminal variants of beta-endorphin. |
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