| Abstract
| - We report here the first documentation that proteins contribute to the scent communication system in a primate. Data presented here indicate that high molecular weight compounds which are not airborne are required for perception of the full attractiveness of the scent. Scent marks from the saddle-back tamarin, a South American primate, contain a number of water-soluble proteins. Gel electrophoresis documents that the major protein (66 kD) is found in urine, and a second protein (18 kD) comes from the gland secretions. The 18 kD protein produces two distinct bands (14 kD and 4 kD) under reducing conditions. Concurrent behavioral studies demonstrate that removal of proteins by enzymatic degradation does not alter the ability of the tamarins to discriminate between scents from different donor types. However, subtle changes in sensory quality occur when the proteins have been degraded. In particular, tamarins do discriminate material in which the proteins have been digested from material in which the proteins are intact. This observation suggests that proteins are a component of what constitutes the scent image. In addition, they may serve as carriers and/or reservoirs for more volatile ligands that encode some of the communicatory messages contained in the material.
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