D'Hondt J, Moens L, Heip J, D'Hondt A, Kondo M
Biochem J. 1978 Jun 1;171(3):705-10. doi: 10.1042/bj1710705.
The oxygen-binding characteristics of the three extracellular haemoglobins of brine shrimp (Artemia salina) were studied in vitro by using highly purified preparations. Haemoglobin I is induced last in the development of brine shrimps when functional gills are formed. It has the lowest oxygen affinity (p(50) 5.34mmHg), an intermediate Bohr effect (ø -0.09 at 20 degrees C) above pH8 and a temperature-sensitivity (DeltaH -44.8 to -45.6kJ/mol at pH8-9) comparable with those observed with other invertebrate haemoglobins [Weber & Heidemann (1977) Comp. Biochem. Physiol. A57, 151-155]. Haemoglobin II, which is the first to be induced, soon after hatching of nauplius larvae, persists generally throughout the whole adult life. It has an intermediate oxygen affinity (p(50) 3.7mmHg), the highest Bohr effect (ø -0.21 at 20 degrees C) above pH8 and a similar temperature-sensitivity (DeltaH -46.0 to -54.8kJ/mol at pH8-9) as haemoglobin I. However, haemoglobin III, which is induced second several hours after the induction of haemoglobin II but disappearing from the haemolymph in the middle of adult life, has the highest oxygen affinity (p(50) 1.8mmHg), the lowest Bohr effect (ø -0.03 at 20 degrees C) above pH8.5 and a high resistance against temperature variation between 10 and 25 degrees C at pH8.5-9 (DeltaH -22.6 to -23.0kJ/mol). At pH7.5-8, haemoglobin III exhibits a similar temperature-sensitivity under 30 degrees C as do other haemoglobins. All three haemoglobins have a rather low co-operativity, with Hill coefficients (h 1.6-1.9 at pH8.5), which are dependent on both pH and temperature. The highest co-operativity was observed at 20 degrees C and pH9 for haemoglobins I and II, whereas it was at 27 degrees C and pH8.5 for haemoglobin III. Thus the oxygen-binding behaviour of haemoglobin III in vitro is significantly different from those of haemoglobins I and II and indicates possibly its specific physiological role in vivo in the adaptive process in the natural environment.
利用高度纯化的制剂,在体外研究了卤虫(卤虫)三种细胞外血红蛋白的氧结合特性。血红蛋白I在卤虫发育过程中形成功能性鳃时最后被诱导产生。它具有最低的氧亲和力(p(50)为5.34mmHg),在pH8以上具有中等的玻尔效应(20℃时ø为-0.09),以及与其他无脊椎动物血红蛋白相当的温度敏感性(pH8 - 9时ΔH为-44.8至-45.6kJ/mol)[Weber & Heidemann (1977) Comp. Biochem. Physiol. A57, 151 - 155]。血红蛋白II是在无节幼体幼虫孵化后不久最早被诱导产生的,通常在整个成年期都存在。它具有中等的氧亲和力(p(50)为3.7mmHg),在pH8以上具有最高的玻尔效应(20℃时ø为-0.21),以及与血红蛋白I相似的温度敏感性(pH8 - 9时ΔH为-46.0至-54.8kJ/mol)。然而,血红蛋白III在血红蛋白II诱导后数小时被诱导产生,在成年期中期从血淋巴中消失,它具有最高的氧亲和力(p(50)为1.8mmHg),在pH8.5以上具有最低的玻尔效应(20℃时ø为-0.03),并且在pH8.5 - 9时对10至25℃之间的温度变化具有高抗性(ΔH为-22.6至-23.0kJ/mol)。在pH7.5 - 8时,血红蛋白III在30℃以下表现出与其他血红蛋白相似的温度敏感性。所有三种血红蛋白的协同性都相当低,希尔系数(pH8.5时h为1.6 - 1.9),其依赖于pH和温度。血红蛋白I和II在20℃和pH9时观察到最高的协同性,而血红蛋白III在27℃和pH8.5时观察到最高协同性。因此,血红蛋白III在体外的氧结合行为与血红蛋白I和II的显著不同,这可能表明其在自然环境中的适应性过程中在体内具有特定的生理作用。