Structural and biophysical characterization of the major proteins from the seminal plasma of Dorper rams
| Autor: | Luan Sitó da Silva, Flavio Augusto Vicente Seixas, Maycon Araújo Ruivo, Eduardo Jorge Pilau, Gentil Vanini de Moraes, Ícaro Putinhon Caruso, Jean Eduardo Meneguello, Antonio Campanha Martinez, Tainá Michelle da Cruz |
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| Přispěvatelé: | Universidade Estadual de Maringá (UEM), Universidade Estadual Paulista (Unesp), Universidade Federal do Rio de Janeiro (UFRJ) |
| Rok vydání: | 2020 |
| Předmět: |
Male
Circular dichroism Animal reproduction Size-exclusion chromatography Spermadhesin Semen Mass spectrometry 03 medical and health sciences 0302 clinical medicine Protein structure Food Animals Pregnancy Animals Centrifugation Amino Acid Sequence Small Animals Peptide sequence Sheep Domestic 030219 obstetrics & reproductive medicine Sheep Equine Chemistry Protein 0402 animal and dairy science Seminal Plasma Proteins Proteins 04 agricultural and veterinary sciences 040201 dairy & animal science Biochemistry Animal Science and Zoology Female Semen Preservation |
| Zdroj: | Scopus Repositório Institucional da UNESP Universidade Estadual Paulista (UNESP) instacron:UNESP |
| ISSN: | 1879-3231 |
| Popis: | Made available in DSpace on 2021-06-25T10:54:23Z (GMT). No. of bitstreams: 0 Previous issue date: 2021-05-01 Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) College of Dentistry, University of Kentucky Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq) Fundação Araucária Pregnancy rates using frozen semen from rams are higher than for horses. One of the factors that positively influences this effect is the composition of low-molecular-weight proteins from seminal plasma, since the amounts of these proteins are much lower in horses. The aim of this work was to purify the major protein components from ram seminal plasma for structural and biophysical characterization. First, the ram semen was collected and the plasma separated by centrifugation. The protein fractions were isolated by gel filtration chromatography, analyzed by circular dichroism spectroscopy and the amino acid sequence identified by mass spectrometry (LC-MSE), the results of which were used to model the protein structure by bioinformatics techniques. This protein was identified by LC-MSE as a spermadhesin, being an unglycosylated monomer with Tm = 69.3 °C and ΔHm = 371 kJ mol−1 at pH 7.0. This work describes for the first time the structural characterization of a spermadhesin from seminal plasma of Dorper rams. Department of Veterinary Medicine Universidade Estadual de Maringá – UEM Department of Technology Universidade Estadual de Maringá – UEM Department of Clinical Analyses and Biomedicine Universidade Estadual de Maringá – UEM Department of Chemistry Universidade Estadual de Maringá – UEM Department of Physics and Biomolecular Innovation Center (CMIB) Instituto de Biociências Letras e Ciências Exatas – IBILCE/UNESP National Center for Nuclear Magnetic Resonance of Macromolecules Institute of Medical Biochemistry and National Center for Structural Biology and Bioimaging (CENABIO) UFRJ Department of Physics and Biomolecular Innovation Center (CMIB) Instituto de Biociências Letras e Ciências Exatas – IBILCE/UNESP Fundação Araucária: 40/16 Fundação Araucária: 53/19 |
| Databáze: | OpenAIRE |
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