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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Gadelha, C. A. Rádis-Baptista, G. Melo, L. M. Cunha, R. M. Teixeira, D. I. Bloch, C. Freitas, V. J. Cavada, B. S. |
| Description | Country affiliation: Brazil Responsible library: BR1.1 Author Affiliation: Teixeira, D. I ( Universidade Estadual do Ceará. Laboratório de Fisiologia e Controle da Reprodução. Fortaleza. BR); Bloch, C ( EMBRAPA. CENARGEN. Laboratório de Espectrometria de Massa. Brasília. BR); Cunha, R. M ( Universidade Federal do Ceará. BioMol-Lab. Fortaleza. BR); Gadelha, C. A ( Universidade Federal do Ceará. BioMol-Lab. Fortaleza. BR); Melo, L. M ( Universidade Federal do Ceará. BioMol-Lab. Fortaleza. BR); Rádis-Baptista, G ( Universidade Federal do Ceará. BioMol-Lab. Fortaleza. BR); Cavada, B. S ( Universidade Federal do Ceará. BioMol-Lab. Fortaleza. BR); Freitas, V. J ( Universidade Estadual do Ceará. Laboratório de Fisiologia e Controle da Reprodução. Fortaleza. BR) |
| Abstract | Mammalian seminal plasma contains among others, proteins called spermadhesins, which are the major proteins of boar and stallion seminal plasma. These proteins appear to be involved in capacitation and sperm-egg interaction. Previously, we reported the presence of a protein related to spermadhesins in goat seminal plasma. In the present study, we have further characterized this protein, and we propose ion-exchange chromatography to isolate this seminal protein. Semen was obtained from four adult Saanen bucks. Seminal plasma was pooled, dialyzed against distilled water and freeze-dried. Lyophilized proteins were loaded onto an ion-exchange chromatography column. Dialyzed-lyophilized proteins from the main peak of DEAE-Sephacel were applied to a C2/C18 column coupled to an RP-HPLC system, and the eluted proteins were lyophilized for electrophoresis. The N-terminal was sequenced and amino acid sequence similarity was determined using CLUSTAL W. Additionally, proteins from DEAE-Sephacel chromatography step were dialyzed and submitted to a heparin-Sepharose high-performance liquid chromatography. Goat seminal plasma after ion-exchange chromatography yielded 6.47 +/- 0.63 mg (mean +/- SEM) of the major retained fraction. The protein was designated BSFP (buck seminal fluid protein). BSFP exhibited N-terminal sequence homology to boar, stallion and bull spermadhesins. BSFP showed no heparin-binding capabilities. These results together with our previous data indicate that goat seminal plasma contains a protein that is structurally related to proteins of the spermadhesin family. Finally, this protein can be efficiently isolated by ion-exchange and reverse-phase chromatography. |
| e-ISSN | 16765680 |
| Journal | Genetics and Molecular Research |
| Issue Number | 1 |
| Volume Number | 5 |
| Language | English |
| Publisher | Fundação de Pesquisas Científicas de Ribeirão Preto |
| Publisher Place | Brazil |
| Access Restriction | Open |
| Subject Keyword | Animals Chromatography, Ion Exchange Semen Chemistry Seminal Plasma Proteins Isolation & Purification Genetics Discipline Genetics Discipline Molecular Biology Discipline Bioinformatics |
| Content Type | Text |
| Resource Type | Article |
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