Abstract
The chemical recognition systems used by aquatic invertebrates to discriminate mates are poorly understood. We describe the results of analysis of a surface glycoprotein that serves as a mate‐recognition pheromone (MRP) for the marine rotifer Brachionus plicatilis. Binding of a polyclonal antibody to the MRP signal on females is described. The binding of anti‐MRP to purified MRP in nitrocellulose membranes is non‐linear. Anti‐MRP also can be used to detect MRP in crude homogenates of rotifer proteins where MRP comprises 0.06 to 0.14% of total protein. As little as 1–2 ng of MRP can be detected in crude homogenates. We estimated that a single B. plicatilis female has about 0.11 ng of MRP concentrated primarily in her corona. Males can discriminate conspecific females from those of other species, females from different geographic populations, and males from females in their own populations. Monosaccharide analysis of the MRP demonstrated the presence of mannose, glucose, N‐acetylglucosamine, fucose, and N‐a...
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