Please use this identifier to cite or link to this item: http://www.repositorio.ufc.br/handle/riufc/59840
Title in Portuguese: Ion-exchange chromatography used to isolate a spermadhesin-related protein from domestic goat (Capra hircus) seminal plasma
Title: Ion-exchange chromatography used to isolate a spermadhesin-related protein from domestic goat (Capra hircus) seminal plasma
Author: Teixeira, Dárcio Ítalo Alves
Melo, Luciana Magalhães
Gadelha, Carlos Alberto de Almeida
Cunha, Rodrigo Maranguape Silva da
Bloch Júnior, Carlos
Rádis-Baptista, Gandhi
Cavada, Benildo Sousa
Freitas, Vicente José de Figueirêdo
Keywords: Plasma seminal
Ovinos
Lecitina
Issue Date: 2006
Publisher: Genetics and Molecular Research
Citation: TEIXEIRA, Dárcio Ítalo Alves; MELO, Luciana Magalhães; GADELHA, Carlos Alberto de Almeida; CUNHA, Rodrigo Maranguape Silva da; BLOCH JÚNIOR, Cunha; RÁDIS-BAPTISTA, Gandhi; CAVADA, Benildo Sousa; FREITAS, Vicente José de Figueirêdo. Ion-exchange chromatography used to isolate a spermadhesin-related protein from domestic goat (Capra hircus) seminal plasma. Genetics and Molecular Research, v. 5, n.1, p. 79-87. 2006 Disponível em: https://www.academia.edu/4589075/Ion_exchange_chromatography_used_to_isolate_a_ spermadhesin_related_protein_from_domestic_goat_Capra_hircus_seminal_plasma. Acesso em: 4 ago. 2021
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 highperformance 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
URI: http://www.repositorio.ufc.br/handle/riufc/59840
metadata.dc.type: Artigo de Periódico
ISSN: 1676-5680
Appears in Collections:LABOMAR - Artigos publicados em revistas científicas

Files in This Item:
File Description SizeFormat 
2006_art_diateixeira.pdf671,89 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.