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Electroolfactogram and electrovomeronasogram recordings were made from garter snakes stimulated with vapor of amyl acetate, butanol and of earthworm wash. The olfactory epithelium was more sensitive than the vomeronasal epithelium to all three stimuli. Volatiles from prey washes were capable of stimulating the olfactory epithelium when delivered as airstreams. The vomeronasal epithelium was sensitive only to the air delivery of vapor of amyl acetate. Single unit recordings from the mitral cell layer of the accessory olfactory bulb of garter snakes were made in response to liquid delivery of a variety of chemical stimuli including classical odorants, amino acids and proteins derived from prey. All three classes of stimuli altered unit firing in the accessory olfactory bulb. Amyl acetate, earthworm wash, goldfish wash and non-volatile amino acids delivered as liquid stimuli to the vomeronasal epithelium produced responses in the accessory olfactory bulb that were more distinct and reliable than the electrovomeronasogram responses to airborne odorants recorded at the periphery. Both excitatory and inhibitory responses were observed in the accessory olfactory bulb of garter snakes. The direction of the response to a given stimulus differed for different neurons. Responses were frequently biphasic and could last longer than 50 seconds. Individual neurons responded to different classes of stimuli suggesting that they are broadly tuned.

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We have isolated seven proteins from earthworm preparations that are chemoattractive to garter snakes. Three of these proteins have been purified to homogeneity: two from aqueous earthworm wash (EWW) and one from electric shock-induced earthworm secretion (ESS). One of the two highly purified proteins from EWW has a relative molecular mass of 20 kDa and contains free sulfhydryl groups that appear to play a functional role in its chemoattractivity. The other purified protein from EWW has a molecular mass of 3 kDa (low molecular weight protein, LMW). The highly purified chemoattractive protein (ES20) from ESS is a glycoprotein having a minimum molecular mass of 15.4 kDa calculated from its amino acid and carbohydrate contents. It consists of a single polypeptide chain. The sequence of terminal 15 amino acid residues from its amino (NH₂–) terminal has been determined. It binds specifically to the membranes of vomeronasal sensory epithelium in a saturable and reversible fashion with a K_d value of about 0.3 µM and B_max value of 0.4 nmol/mg of protein. This protein causes an increase in firing rate of individual neurons in the accessory olfactory bulb of garter snakes, the projection site for vomeronasal neurons. All the isolated chemoattractive proteins from both earthworm preparations can be divided immunologically into three groups: (i) those closely related to the ES20 snake-attractive protein, (ii) those closely related to the LMW snake-attractive protein, and (iii) those unrelated to either ES20 or the LMW protein.