Intracellular ph in cold-blooded vertebrates as a function of body temperature
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Cited by (90)
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2022, Progress in Biophysics and Molecular BiologyCitation Excerpt :In fact, it has been shown that the pH of frog muscle changes as a function of temperature. It is about 7.4 at 4 °C and about 6.9 at 37 °C, i.e., about half a pH unit between the two temperatures ((Marjanovic et al., 1998)) (Malan et al., 1976). report a pH-change of −0.0147 pH units per degree in frog muscle.
The influence of assisted ventilation and recumbency on cardiorespiratory physiology in the anesthetized freshwater turtle Trachemys scripta scripta
2021, Comparative Biochemistry and Physiology -Part A : Molecular and Integrative PhysiologypH regulation in hibernation: Implications for ventilatory and metabolic control
2019, Comparative Biochemistry and Physiology -Part A : Molecular and Integrative PhysiologyCitation Excerpt :For example, the active site of lactate dehydrogenase requires protonated histidine residues to bind its substrate pyruvate. Regulating αim in vitro has been shown to reduce the changes in Michaelis–Menten constant (Km; the concentration of substrate at which the rate of enzymatic reaction is half of maximum rate) of lactate dehydrogenase with decreasing temperature (Yancey and Somero, 1978) and alpha-stat regulation of intracellular pH (pHi) has been demonstrated in various tissues of heterothermic vertebrates (Malan et al., 1976; Walsh and Moon, 1983; Bock et al., 2001). Air-breathing vertebrates generally maintain an extracellular pH (pHe) that is alkaline relative to pHnw, but the degree of relative alkalinity varies between vertebrate groups.
The cooperative actuation of multistep electrochemical molecular machines senses the working temperature: voltammetric study
2017, Electrochimica ActaCitation Excerpt :In addition, those muscles sense by themselves the chemical and physical working conditions while actuating: they are haptic muscles [3]. The environmental temperature has a strong influence on the muscular reactions of any cold-blooded animal (ectotherm) [4–8]. The underlying working mechanism and the origin of the awareness of the thermal working conditions, remains as a controversial subject.
A critical evaluation of automated blood gas measurements in comparative respiratory physiology
2014, Comparative Biochemistry and Physiology -Part A : Molecular and Integrative PhysiologyCitation Excerpt :The apparent similarity in temperature dependency among turtle, snake and human blood, indicates that potential differences in non-bicarbonate buffer capacity caused by differences in the number of histidine residues in proteins and the total protein concentration (see Jensen, 1989; Berenbrink, 2006) had negligible effects on the pH temperature dependency (i.e. Rosenthal, 1948; Reeves, 1976). The pH temperature dependency of human blood has been reported to be − 0.0147 pH°C− 1 (Rosenthal, 1948), while a value of − 0.0207 pH°C− 1 was found for T. scripta (Malan et al., 1976). This fits well with the present data as the error between GEM pH and BMS pH caused by the slight displacement of the regression is around .05 pH units (Table 2 and Fig. 6).
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Present address: CNRS, Laboratoire de Physiologie Respiratoire, 67087 Strasbourg, France.