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Journal of Experimental Biology, Vol 201, Issue 23 3233-3244, Copyright © 1998 by Company of Biologists
JOURNAL ARTICLES |
AM Adamczewska and S Morris
School of Biological Sciences (A08), University of Sydney, Sydney, NSW 2006, Australia. ishka@oimb.uoregon.edu.
Gecarcoidea natalis is a land crab that migrates annually several kilometres to breed. The O2-binding properties of haemocyanin in G. natalis were investigated in vitro to test the idea that the O2-binding properties of the haemocyanin of land crabs are not dependent on circulating modulators and to provide a model of haemocyanin functioning during exercise. The affinity of the haemocyanin for O2 decreased with increasing temperature (change in the heat of oxygenation; capdelta H=-59 kJ mol-1). The haemocyanin of G. natalis apparently differs from that of other terrestrial crabs in showing haemocyanin O2 modulation by both organic and inorganic molecules. Haemocyanin O2-affinity was not affected by Mg2+ but was sensitive to changes in Ca2+ concentration ( capdelta logP50/ capdelta log[Ca]=-0.61, where P50 is the partial pressure of O2 required for half-maximal O2 binding). The Bohr factor was modest ( &phgr; =-0.26+/-0.03, N=4, in whole haemolymph at 25 degreesC) and there was no specific effect of CO2 on the O2-binding properties of the haemocyanin. An increase in urate concentration increased haemocyanin O2-affinity, but the effect was linear ( capdelta logP50/ capdelta [urate]=-0.06) and not logarithmic as is the case in other species. The effect of l-lactate on the haemocyanin O2-affinity in G. natalis was unique among the crustaceans, because an increase in l-lactate concentration decreased the haemocyanin O2-affinity. The effect of l-lactate on haemocyanin O2-affinity ( capdelta logP50/ capdelta log[lactate]) was time-dependent and decreased from a maximum of 0.044 on day 1 to 0.001 after 4 days of storage at 4 degreesC. The presence of an unknown dialysable and unstable factor in the haemolymph is postulated to explain the time-dependent effect of l-lactate on haemocyanin O2-binding properties. Model oxygen equilibrium curves constructed for in vivo conditions showed that the reverse effect of l-lactate was advantageous by decreasing the O2-affinity of the haemocyanin beyond that predicted by the Bohr shift alone and assisted in O2 off-loading at the tissues. This effect of lactate can only provide an advantage if the gas-exchange organs maintain arterial O2 loading and thus is dependent on lung function in land crabs and must have occurred coincident with the evolution of these other features.
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