Oxygen binding in alligator blood related to temperature, diving, and "alkaline tide".

Oxygen binding in alligator blood related to temperature, diving, and "alkaline tide".
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鳄鱼血液中的氧结合与温度、潜水和“碱潮”有关。

DOI:
10.1152/ajpregu.1986.251.5.r901
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发表时间:
1986
期刊:
The American journal of physiology
影响因子:
--
通讯作者:
White,FN
White,FN
中科院分区:
--
文献类型:
--
作者:
Weber,RE;White,FN

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密西西比短吻鳄的血液具有相对高的O2亲和力,在pH 7.495时半饱和O2张力(P50)= 24.5 Torr,在25 ℃时动脉正常碳酸pH。尽管P50在15、25和35 ℃和恒定pH下的总体温度敏感性较低,但在每个温度的体内pH下测量时,对P50的影响几乎加倍(Δ Happ分别= -24和-47 kJ/mol)。CO2玻尔效应(θ CO2 = -0.95)是固定酸玻尔效应(θ FA)的5.5倍,而Haldron效应很小(约0.03 pH单位)。相对较高的O2亲和力可以确保在屏气和潜水期间有效利用肺O2储备,而其显著的体内温度敏感性可以适应器官O2需求的高温环境。θ CO2和θ FA之间的巨大差异将有利于在面对大量活动诱导的血乳酸增加和明显的进食诱导的血糖升高时血液O2亲和力的恒定性。这些“碱性潮汐”是由血浆Cl-交换为穿过肠壁的HCO-3而产生的,似乎仅通过增加的血液CO2张力而轻微补偿。另外讨论的结果在变构调制血红蛋白-O2的亲和力在crococoanans。
Blood of Alligator mississippiensis has a relatively high O2 affinity, the half-saturation O2 tension (P50) = 24.5 Torr at pH 7.495, the arterial, normocapnic pH at 25 degrees C. Although the overall temperature sensitivity of P50 at 15, 25, and 35 degrees C and constant pH is low, the effect on P50 almost doubles when measured at the in vivo pH of each temperature (delta Happ = -24 and -47 kJ/mol, respectively). The CO2 Bohr effect (theta CO2 = -0.95) is 5.5 times greater than the fixed acid Bohr effect (theta FA), and the Haldane effect is small (approximately 0.03 pH units). The relatively high O2 affinity may ensure efficient utilization of the lung O2 reserve during breath holding and diving, whereas its pronounced in vivo temperature sensitivity may be adaptive to the high temperature quotients of the organismic O2 requirement. The large difference between theta CO2 and theta FA will favor constancy in blood O2 affinity in the face of large activity-induced increases in blood lactate and pronounced feeding-induced alkaloses. These "alkaline tides," which result from an exchange of plasma Cl- for HCO-3 across the gut wall, appear to be only slightly compensated by increased blood CO2 tensions. The results are additionally discussed in terms of allosteric modulation of hemoglobin-O2 affinity in crocodilians.
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