The degree of polymorphism and heterozygosity in the striped hermit crab, Clibanarius vittatus (Bosc) (Decapoda:Anomura), from the Texas coast

Abstract

Two populations of Cilbanarius vittatus (Bosc), the striped hermit crab, were sampled, one from Bolivar and the other from Port Isabel, Texas, in order to compare their degrees of polymorphism and heterozygosity with respect to the following enzymes: lactate dehydrogenase (LDH), glucose-6-phosphate (G6PDH), malate dehydrogenase (MDH), xanthine dehydrogenase (XDH), and tetrazolium oxidase (TO). The enzymes were separated by means of starch gel electrophoresis and identified by means of substrate-specific stains. An investigation was also made on LDH to determine tissue specificity and the isozyme patterns produced by various tissues. The fastest of the six bands of activity, designated LDH-3, was found only in extracts from gonad tissue and was inferred to be encoded by a single locus, Ldh-3. The slowest moving one (LDH-1) was considered to be a homotetramer composed of subunits encoded by the Ldh-1 locus, and the second fastest one (LDH-2) was considered to be a homotetramer composed of subunits encoded by the Ldh-2 locus. The three intermediate bands were concluded to be heterotetramers composed of different combinations of the two subunits. LDH-1 predominated in abdominal muscle, and LDH-2 predominated in claw and heart muscles..