Characterization of vitellogenin and its derived yolk proteins in cloudy catshark (Scyliorhinus torazame)
| Autor: | Rieko Sugawara, Akihiko Hara, Osamu Nishimiya, Takahiro Matsubara, Toshiaki Fujita, Naoshi Hiramatsu, Haruna Amano, Tomoki Yagai, Takashi Todo, Kodai Yamane |
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| Rok vydání: | 2012 |
| Předmět: |
food.ingredient
DNA Complementary Physiology Blotting Western Molecular Sequence Data Aquatic Science Phosvitin Biochemistry Vitellogenin Vitellogenins food Yolk Complementary DNA Animals Cluster Analysis Amino Acid Sequence Phylogeny DNA Primers Chromatography biology Base Sequence Egg Proteins Protein primary structure Computational Biology General Medicine Anatomy Sequence Analysis DNA biology.organism_classification Molecular biology Scyliorhinus torazame Catshark Molecular Weight biology.protein Chromatography Gel Sharks Electrophoresis Polyacrylamide Gel Vitellogenesis |
| Zdroj: | Fish physiology and biochemistry. 39(2) |
| ISSN: | 1573-5168 |
| Popis: | Elasmobranchs (sharks and rays) exhibit unique reproductive characteristics and, in contrast to the situation in teleosts, very little is known about the identity, structure and physical characteristics of their egg yolk proteins. The aims of this study were to (1) detect and purify the vitellogenin (Vtg; egg yolk precursor) and yolk proteins (YPs) of the cloudy catshark (Scyliorhinus torazame), (2) examine the relationships between Vtg and YPs and (3) characterize and classify the deduced primary structure of the Vtg transcript (vtg). The apparent molecular weights of purified Vtg and putative Vtg-related YPs (lipovitellin: Lv, phosvitin: Pv) were determined by gel filtration and were ~560, >669 and ~58 kDa, respectively. Following SDS-PAGE, these purified products (i.e., Vtg, Lv and Pv) appeared as bands of ~210, ~110 and ~22 kDa, respectively. On Western blots, antisera against purified Vtg, Lv and Pv recognized the ~210 kDa Vtg band. Catshark Pv, in contrast to teleost Pvs, had a very low serine content. The catshark Vtg cDNA sequence (vtg) appeared to contain an open-reading frame consisting of domains encoding Lv, Pv and β′-component (β′-c). A phylogenetic analysis, with a consideration of genome duplication events, placed catshark vtg into the ‘vtgAB type.’ It is concluded that at least a single major type of Vtg protein, which is transcribed and translated from catshark vtgAB gene, is the precursor of three egg yolk proteins (Lv, Pv and β′-c) in catshark. |
| Databáze: | OpenAIRE |
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