Genetic Polymorphism of Boar Seminal Plasma Proteins

Proteomics of boar seminal plasma

Extensive dataset of boar seminal plasma proteome displaying putative reproductive functions of identified proteins

A complete proteomic profile of seminal plasma (SP) remains challenging, particularly in porcine. The data reports on the analysis of boar SP-proteins by using a combination of SEC, 1-D SDS PAGE and NanoLC-ESI-MS/MS from 33 pooled SP-samples (11 boars, 3 ejaculates/boar). A complete dataset of the 536 SP-proteins identified and validated with confidence ≥95% (Unused Score >1.3) and a false disc...

Protein analysis of boar seminal plasma proteins with protective effect during low-temperature storage of spermatozoa

The present study aimed to investigate the effect of different seminal plasma proteins (SPPs) on boar spermatozoa functional characteristics. We investigated the putative protective effect of SSPs on sperm cells motility and velocity, as well as on the integrity of the plasma membrane (PM) during low-temperature storage at 4 °C. SPPs fractions were obtained and purified by gel permeation chroma...

The ability of zinc-binding proteins from boar seminal plasma to bind heparin and phosphorylcholine*

Zinc-binding proteins (ZnBPs) isolated from boar seminal plasma exert multiple effects on boar spermatozoa. The aim of this study was to determine whether the isolated zinc-binding proteins were capable of binding additional ligands. The affinity chromatography method was used for the first time to demonstrate that boar ZnBPs show affinity for both heparin (hep) and phosphorylcholine (pch). ZnB...

The Proteins of Bovine Seminal Plasma

Experiments have been reported in Paper I (1) in which the proteins of bovine seminal plasma were subjected to preliminary and electrophoretic characterization. In order to characterize this protein system further, ultracentrifugal and immunological methods have been applied. A limited amount of work has been reported on the ultracentrifugation of the seminal plasma proteins. Ross (2) has noted...