| Abstract: | Three proteins related to the hamster vaginal discharge proteinaphrodisin were purified, subjected to adsorption chromatographyfor removal of volatile compounds and tested for pheromonalactivity in an assay of copulatory behavior exhibited by malehamsters toward a surrogate female. One of the proteins is conspecificto aphrodisin, it is the second most abundant protein in thevaginal discharge. Like aphrodisin it migrates as a relativelyacidic protein in electrophoresis under non-denaturing conditions,and it appears to have an identical monomeric molecular mass(17 kd) in electrophoresis with 0.1% sodium dodecylsulfate.Heterospecific proteins included the female mouse major urinaryprotein (MUP) and ß-lactoglobulin from cow's milk,which have some similarity in amino acid sequence to aphrodisinand belong to the  2u-globulin protein superfamily. In spiteof these chemical relationships, neither the conspecific proteinnor the heterospecific proteins had aphrodisiac activity comparableto that of aphrodisin in the surrogate female behavioral assay.The pheromonal activity of aphrodisin thus appears to be dependenton specific structural features of the protein. |
