Circular Dichroism of Pig and Bovine Lactadherins and Their Affinity for the Pig Zona Pellucida

Zayas-Pérez, H; Tello-Solís, Salvador R.; González‐Márquez, Humberto; Bonilla-González, Edmundo; Mendoza‐Hernández, Guillermo; Betancourt-Rule, Miguel

doi:10.2174/0929866053587084

Cited by 1 publication

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“…A 48 kDa band was also found in capacitated sperm, and by the limited sequence obtained, could be lactadherin. Our results agree with those by Petrunkina et al [22], who reported the presence of lactadherin in the acrosomal region of boar sperm, and with those by Zayas-Perez et al [36], who isolated porcine and bovine milk lactadherins by affinity chromatography using ZP as ligand.…”

Section: Discussionsupporting

confidence: 93%

Carbohydrate Affinity Chromatography Indicates That Arylsulfatase-a From Capacitated Boar Sperm Has Mannose and N-Acetylglucosamine/Sialic Acid Residues

Jiménez

Fierro

González‐Márquez

et al. 2006

Archives of Andrology

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Carbohydrate residues on membrane proteins from sperm are important in gamete interaction. In recent years, Arylsulfatase A (AS-A) has been acquiring an important role from the various putative gamete interaction responsibles in sperm. The aim of this study was to determine if the capacitated boar sperm Arylsulfatase-A (AS-A), contains D-mannose, N-acetylglucosamine and/or sialic acid residues by its purification using affinity chromatography with Concanavalia ensiformis Agglutinin(Con-A) or Wheat Germ Agglutinin (WGA) as ligands. Sperm samples were capacitated in TALP-HEPES medium. Protein extract was added to the affinity columns. Sequencing of retained proteins was done after SDS-PAGE. Total capacitated sperm proteins electrophoresis showed molecular masses between 14 kDa and 102 kDa. A major band of 68 kDa, and 2 minor bands of 52 kDa and 47 kDa were observed. They were AS-A, hyaluronidase and lactadherin, respectively. The Con-A-retained proteins (RP) pattern showed bands from 14 to 98 kDa. After sequencing and BLAST analysis, the 62 kDa band corresponded to Arylsulfatase-A. The WGA RP fraction showed bands from 14 to 100 kDa. The 65 kDa band corresponded to AS-A. This study showed that AS-A has mannose, N-acetylglucosamine and/or sialic acid residues as part of its glycosilation. In this study AS-A was isolated from boar capacitated sperm by affinity chromatography using separately Con-A and WGA, indicating that there are mannose, N-acetylglucosamine and/or sialic acid residues in its glycosilation. AS-A is a membrane protein of capacitated sperm. Further investigation is needed to fully characterize the glycosidic residues bore by AS-A and to determine its function.

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Section: Discussionsupporting

confidence: 93%