Hb Lab Report

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Introduction
Oxygen circulation throughout the body is carried out through haemoglobin, a complex tetramer protein with more than 140 amino acids and the ability to bind to up to four oxygen atoms (Protein Data Bank – ID 1GZX). Haemoglobin (Hb) first binds to a single oxygen molecule (O2), which brings about a conformational change in the Hb molecule, causing three additional O2 molecules to bind to it (Jensen et al., 2016). Hb is present in red blood cells, which are the medium for O2 transport to the tissues of the body. The amount of O2 bound to Hb depends on the partial pressure of O2, or the pressure of pure oxygen gas within a given volume. At a partial pressure of P50, 50% of the Hb is saturated with O2, leaving room for 50% of the remaining Hb to be occupied by CO2 (Dash and Bassingthwaighte, 2010). In this regard, both O2 and CO2 inversely affect each other’s affinity for Hb.
The oxygen-haemoglobin binding effect is plotted in …show more content…
For the acidic blood pH, the partial pressure of oxygen required for 50% Hb saturation (P50) was higher than that for the basic pH. This means that there was a greater amount of O2 needed to saturate the Hb at lower pH blood, as compared to the higher pH blood, to the same degree of saturation.
These results have also been demonstrated in numerous research articles. Giardina et al. (2016) analyzed blood from over eleven different vertebrates from many different research articles, at multiple different pH levels, and observed an oxygen dissociation curve similar to that constructed in this experiment, with the oxygen dissociation curves shifting to the right as pH decreased. In the alligator, for example, lower pH levels showed lower Hb saturation levels, and lower P50 levels. These results are consistent with this experiment, as well as the Bohr

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