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Table S1. Character matrix for protein bands in a 15% Tricine SDS-PAGE gel ranging from 9 to 125 kD.

Table S2. Differences in protein bands found among the ‘Tasmania’ species.

Table S3. Character matrix for protein bands in a 4% Tricine SDS-PAGE gel ranging from 350 to 1300 kD.

Table S4. Character matrix for protein bands in a 14% Tricine SDS-PAGE gel ranging from 55 to 110 kD.

Table S5. Character matrix for protein bands in a 14% Tricine SDS-PAGE gel ranging from 8 to 25 kD.

Table S6. Differences in protein bands found among the twelve species studied.

Table S7. Presence–absence matrix used for the maximum parsimony analysis (branch-and-bound search).

Fig. S1. Intraspecifically conserved protein composition in onychophoran slime. Non-reduced 14% T, 3% C Tricine SDS-PAGE, silver stain. Positions of molecular mass standards (in kD) are indicated in the left column. Lane numbers are given as follows: 1 and 2, Tasmanipatus anophthalmus; 3 and 4, Tasmanipatus barretti; 5 and 6, Ooperipatellus sp.; 7 and 8, Ooperipatus hispidus. Note the highly conserved protein band patterns within the same species.

Fig. S2. Intraspecifically conserved protein composition in onychophoran slime. Non-reduced 14% T, 3% C Tricine SDS-PAGE, silver stain. Positions of molecular mass standards (in kD) are indicated in the left column. Lane numbers are given as follows: 1 and 2, Principapillatus hitoyensis; 3 and 4, Epiperipatus sp.; 5 and 6, Ooperipatus oviparus; 7 and 8, Ooperipatellus insignis. Note the highly conserved protein band patterns within the same species.

Fig. S3. Intraspecifically conserved protein composition in onychophoran slime. Non-reduced 14% SDS-PAGE, Coomassi stain. Positions of molecular mass standards (in kD) are indicated on the left column. Lane numbers are given as follows: 1 and 2, Euperipatoides rowelli; 3 and 4, Phallocephale tallagandensis. Note the highly conserved protein band patterns within the same species.

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