title: Effect of temperature on pH and electrolyte concentration in air-breathing ectotherms.
abstract: The aim of this study was to determine the effects of temperature upon pH, protein charge and acid-base-relevant ion exchange in air-breathing ectotherms. Plasma and skeletal muscles in cane toads (Bufo marinus) and bullfrogs (Rana catesbeiana) were examined at 30, 20 and 10 degrees C. In addition, skeletal muscle ion concentrations were examined in black racer snakes (Coluber constrictor) at 30 and 10 degrees C. Cooling the amphibians produced a reduction in most of the plasma ion concentrations (Na(+), K(+), Ca(2+), Cl(-), SO(4)(2)(-)) and in protein concentration because of increased hydration. Between 30 and 10 degrees C, total plasma osmolality fell by 14 % in the toads and by 5 % in the frogs. Plasma protein charge, calculated using the principle of electroneutrality, was unaffected by temperature, except possibly for the toads at 10 degrees C. The in vivo skeletal muscle capdelta pHi/ capdelta T ratio, where pHi is intracellular pH and T is temperature, between 30 and 20 degrees C averaged -0.014 degrees C(-)(1) in the toads and -0.019 degrees C(-)(1) in the frogs. Between 20 and 10 degrees C, there was no change in pHi in the toads and a -0.005 degrees C(-)(1) change in the frogs. The in vitro skeletal muscle capdelta pHi/ capdelta T averaged -0.011 degrees C(-)(1) in both toads and frogs. In all three species, skeletal muscle inulin space declined with cooling. Intracellular ion concentrations were calculated by subtracting extracellular fluid ion concentrations from whole-muscle ion concentrations. In general, temperature had a large effect upon intracellular ion concentrations (Na(+), K(+), Cl(-)) and intracellular CO(2) levels. The relevance of the changes in intracellular ion concentration to skeletal muscle acid-base status and protein charge and the possible mechanisms producing the adjustments in intracellular ion concentration are discussed. It is concluded that ion-exchange mechanisms make an important contribution to adjusting pH with changes in temperature.
authors.affiliation: Department of Biology, University of Akron, Akron, OH 44325-3908, USA. Jstinner@uakron.edu
authors.forename: J N
authors.initials: JN
authors.lastname: Stinner
authors.forename: L K
authors.initials: LK
authors.lastname: Hartzler
mesh_terms: D000136:Acid-Base Equilibrium / Q000502:physiology; D000388:Air; D000818:Animals; D001831:Body Temperature / Q000502:physiology*; D002024:Bufo marinus / Q000378:metabolism / Q000502:physiology*; D017812:Colubridae / Q000378:metabolism / Q000502:physiology*; D004560:Electricity; D004573:Electrolytes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D017136:Ion Transport / Q000502:physiology; D018482:Muscle, Skeletal / Q000378:metabolism; D011506:Proteins / Q000737:chemistry; D011892:Rana catesbeiana / Q000378:metabolism / Q000502:physiology*; D012119:Respiration
chemical_list: D004573:Electrolytes; D011506:Proteins