1988] 
Hagen, Smith, & Rissing — Two desert ants 
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plate in tap water to remove unreacted dye. Precipitated dye 
remains in the cellulose acetate layer, so stained plates were pre- 
served directly or photocopied. Genetic interpretations of variation 
in resulting bands was based on known enzyme quaternary structure 
(Harris and Hopkinson 1978, Richardson et al. 1986), supplemented 
by comparison of haploid males where possible. 
We resolved allozyme products of 18 presumptive genetic loci 
from V. pergandei queens, 4 of which were polymorphic with 2 
alleles each: Est-1 and Est-2 (general esterase; beta-naphthyl acetate 
as substrate), Mdh-1 (malate dehydrogenase, EC 1.1.1.37) and Pgm 
(phosphoglucomutase, EC 2.7.5. 1). Optimal separation for the V. 
pergandei esterase allozymes was given by buffer I (25 min at 250 
V); for Mdh-1 by buffer C (30 min at 250 V); and for Pgm by buffer 
I (25 min at 250 V). An additional polymorphism for Idh-1 (isoci- 
trate dehydrogenase, EC 1.1.1.42) was present in one small sample 
(buffer I, 20 min at 250 V). Banding patterns and allele designations 
for the esterase loci are shown in Figure 1; esterase genotypes could 
not be scored from all individuals. 
Figure 1. Zymogram of esterase loci in V. pergandei. Alleles for Est-1 are 
designated “C” (cathodal) and “A” (anodal); the enzyme behaves as a monomer. 
Est-1 CC and CA genotypes are distinguished by the relative intensity of each band, 
since an artifact band comigrates with the A allozyme. Est-2 has alleles “F” (fast) and 
“S” (slow) and behaves as a dimer. “O” = origin; “+” = anodal. For Est-1, lanes, 2, 5, 
6, and 11 are “A/ A”; lanes 1, 3, 4, 7, 8 and 10 are “A/C” and lane 9 is “C/C”. For 
Est-2 lanes 2-6, 7, 10 and 11 are “F/F” and lanes 1, 7, 9 and 12 are “F/S”. 
