Dlouhá H, Donselaar Y, Teisinger J, Vyskocil F
Physiol Bohemoslov. 1980;29(6):543-52.
The activity of membrane Na+--K+-ATPase and electrogenic ionic pump was estimated by biochemical and electrophysiological techniques on diaphragm muscles of mouse and non-hibernating golden hamster between 5 degrees C to 37 degrees C. The electrogenic capacity of ionic pump (measured as maximum hyperpolarization after adding 5 nmol/l K+ to Na+-enriched muscle) was highest at 37 degrees C for the mouse and between 25--30 degrees C for the golden hamster. At lower temperatures (15 degrees C--5 degrees C), the hyperpolarization after adding K+ reversed to depolarization between 15 degrees C and 10 degrees C in the case of the mouse. In the hamster, the slight hyperpolarization persisted even at 5 degrees C. With decreasing temperature, the activity of membrane ATPase of mouse and hamster membrane fraction decreased in both cases to the same extent between 37--25 degrees C. Within the temperature range between 10 degrees C and 5 degrees C the activity of this enzyme of hamster preparations was about 2.4 times higher than in the case of the mouse. In the mouse Na+-enriched diaphragm, ouabain (10(-4) mol/l) decreased the resting membrane potential (RMP) in a K+-free solution at 20 degrees C by about 5 mV, but in the golden hamster preparation, ouabain in the same concentration increased RMP of Na+-enriched diaphragm fibres by more than 5 mV. The activity of membrane ATPase of hamsters was increased by 10(-4) mol/l ouabain more than 2.5 times in a K+-free reaction medium, whereas in the case of the mouse no change of enzyme activity was observed. This indicates that ouabain can be substituted for potassium as an activator of membrane ATPase in the sarcolemma of golden hamster muscle fibres.
采用生化和电生理技术，在5℃至37℃之间对小鼠和非冬眠金黄地鼠的膈肌进行研究，以评估膜Na⁺ - K⁺ - ATP酶和生电离子泵的活性。离子泵的生电能力（以向富含Na⁺的肌肉中添加5 nmol/L K⁺后测得的最大超极化表示）在37℃时小鼠最高，在25 - 30℃时金黄地鼠最高。在较低温度（15℃ - 5℃）下，添加K⁺后的超极化在15℃至10℃之间小鼠出现逆转，变为去极化。在金黄地鼠中，即使在5℃时仍存在轻微超极化。随着温度降低，小鼠和金黄地鼠膜组分的膜ATP酶活性在37 - 25℃之间均以相同程度下降。在10℃至5℃的温度范围内，金黄地鼠制剂中该酶的活性比小鼠高约2.4倍。在20℃无K⁺溶液中，哇巴因（10⁻⁴ mol/L）使富含Na⁺的小鼠膈肌静息膜电位（RMP）降低约5 mV，但在金黄地鼠制剂中，相同浓度的哇巴因使富含Na⁺的膈肌纤维RMP升高超过5 mV。在无K⁺反应介质中，10⁻⁴ mol/L哇巴因使金黄地鼠的膜ATP酶活性增加超过2.5倍，而小鼠的酶活性未观察到变化。这表明在金黄地鼠肌纤维肌膜中，哇巴因可替代钾作为膜ATP酶的激活剂。
