Carbonic Anhydrase in the Accessory Boring Organ of the Gastropod, Urosalpinx

Carbonic anhydrase (CA), the enzyme which catalyzes the reactionCO₂+H₂OH₂CO₃, was found in both active and resting accessoryboring organs (ABO) of Urosalpinx, using a modification of theWaldeyer and Häusler (1959) technique in which the tissuesection is floated on the substrate solution. The intense reactivityof this gland exceeded the activity of other pedal tissues ofthis muricid gastropod. The ventral pedal gland of the femalealso exhibited strong activity, but theconcentration in thistissue was not as intense as that observed in the ABO. No discernible differences between the microvilli of restingand boring ABOs were noted after fixation in acetone, formalin,or glutaraldehyde. However, notable nuances in reactivity ofthe pedal structures occurred when the comparative effect offixatives was evaluated. All variations of the immersion technique, as opposed to flotationprocedures, exhibited a strong stain only in the microvilliof active ABOs, and little or no activity in resting ABOs. Thisdifference between active and resting ABOs (immersion techniqueonly) appears to be due to the binding (chelation) of calciumwith subsequent replacement of cobalt (probably as a carbonatecomplex) in the substrate. The markedly greater CA activity in the ABO, relative to othersecretory tissues inthe snail, suggests a vital role for thisenzyme in the process of penetrating shell. Thelow pH of thesecretion from the active ABO during boring indicates that atleast one phase of the boring process is a chemical reactionassociated with production of acid.