在低氧分压气相平衡状态下，一氧化碳与血红蛋白和肌红蛋白的结合。

CO binding to hemoglobin and myoglobin in equilibrium with a gas phase of low PO2 value.

作者信息

Agostoni A, Perrella M, Sabbioneda L, Zoni U

机构信息

Clinica Medica (V), University of Milan, Italy.

出版信息

J Appl Physiol (1985). 1988 Dec;65(6):2513-7. doi: 10.1152/jappl.1988.65.6.2513.

DOI:10.1152/jappl.1988.65.6.2513

PMID:3215851

Abstract

The aim of this paper was to measure the binding of CO to myoglobin and hemoglobin at various PO2 values. For this purpose we have studied an "in vitro" system made up of solutions of hemoglobin and myoglobin equilibrated in two connected tonometers with the same gas phase of various PO2 and PCO. The results indicate that a significant proportion of CO is released by hemoglobin and binds myoglobin at low PO2 values (approximately 2-3 Torr), in qualitative agreement with the predictions of a previous computer simulation of the "in vivo" system.

摘要

本文的目的是测量在不同氧分压（PO2）值下一氧化碳（CO）与肌红蛋白和血红蛋白的结合情况。为此，我们研究了一个“体外”系统，该系统由血红蛋白和肌红蛋白溶液组成，在两个相连的压力计中平衡，压力计具有相同的不同PO2和PCO的气相。结果表明，在低PO2值（约2 - 3托）时，相当一部分CO从血红蛋白中释放出来并与肌红蛋白结合，这与之前对“体内”系统的计算机模拟预测在定性上是一致的。