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血红蛋白是否存在最佳的P50?关于氧合血红蛋白解离曲线左移或右移的意义的思考。

Is there an optimal P50 of haemoglobin? Considerations about the significance of a left- or right-shift of the oxyhaemoglobin dissociation curve.

作者信息

Sold M J

出版信息

Anaesthesia. 1982 Jun;37(6):640-5. doi: 10.1111/j.1365-2044.1982.tb01275.x.

Abstract

The effect a permanent change in the oxygen-haemoglobin affinity would have on the oxygen transport system is considered theoretically. The calculations were based on Hill's equation and its derivative. It was demonstrated that in normoxia and at normal oxygen consumption the position of the oxyhaemoglobin dissociation curve of the human adult (P50 3.53 kPa) differs from the optimal position calculated and that a right-shift (increase in P50) would be favourable. However, the higher the oxygen consumption and therefore the saturation change, and/or the more pronounced the hypoxia, the more the P50 found in vivo coincides with the theoretical optimum.

摘要

理论上考虑了氧与血红蛋白亲和力的永久性变化对氧运输系统的影响。计算基于希尔方程及其导数。结果表明,在常氧和正常氧消耗情况下,成年人类氧合血红蛋白解离曲线的位置(P50为3.53 kPa)与计算出的最佳位置不同,右移(P50增加)将是有利的。然而,氧消耗越高,因此饱和度变化越大,和/或缺氧越明显,体内发现的P50就越接近理论最佳值。

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