W. P. Hunt

TL;DR: This study is the first to analyze, in a comprehensive way, the origins of tightly bound sperm polypeptides from a single species, and major contributions to the sperm PMPolypeptide profile occurred at ejaculation.

TL;DR: Washed ejaculated boar sperm and sperm from the cauda epididymis bind to the zona pellucida of fixed porcine eggs in large numbers and an earlier observation that antibodies raised against uncapacitated sperm plasma membranes block sperm-egg binding in vivo suggest that this component may be involved in sperm zona interaction in vivo.

TL;DR: A high resolution, two-dimensional (2-D) electrophoretic map of the plasma membrane (PM) polypeptides from the ejaculated boar spermatozoon is described and the catalogue of properties of major Coomassie-stained PM polyPEptides provides a reference for future studies in the boar and other species.

TL;DR: Since anti-APz monovalent antibody raised from whole cauda or corpus sperm plasma membranes or from chromatographic fractions containing APz completely block capacitated sperm from binding to eggs, and since the ability of this antibody to be absorbed develops as sperm become capable of binding to Eggs, APz is view to be the major and perhaps only plasma membrane protein involved in the adhesion of capacitated boar sperm to eggs prior to the acrosome reaction.

TL;DR: Fraction IV PMPs lost the ability to inhibit directly the binding to eggs when treated with chaotropic agents and trypsin; the fraction also displayed a tendency to aggregate in the absence of high salt, indicating that specific hydrophilic interactions may play a significant role in sperm-zona attachments.