Question

It is possible to observe the effect of oxygenation of hemoglobin in an unbuffered solution in distilled water, but it is more common to measure the effect of pH in a bicarbonate-buffered solution (like plasma) on the oxygen affinity of the protein. These are actually the two ways in which the Bohr effect was first described. From what you know about the origin of the Bohr protons, which statement is correct? A. the pH of the hemoglobin solution would go up when oxygen is bound, regardless of whether it was buffered or not. B. the pH of the hemoglobin solution would go down when oxygen is bound, regardless of whether it was buffered or not. C. the unbuffered hemoglobin solution would become more acidic as oxygen is bound while the affinity of the buffered hemoglobin solution for oxygen would increase as the pH was lowered. D. the unbuffered hemoglobin solution would become more acidic as oxygen is bound while the affinity of the buffered hemoglobin solution for oxygen would decrease as the pH was lowered. E. none of the above observations is correct for the effects of oxygenation and pH on unbuffered and buffered solutions of hemoglobin.
biochem help. could i get an explaination on how to get the right answer plz.

Answer 1

Answer : (c)

Affinity of buffered hemoglobin will increase for oxygen when pH is lowered as buffer can sequester increased protons or H+ ions of added acid and Hemoglobin may be free to bind oxygen

More explanation follows:

TExplanoton Tssues HOWhomagesb Canbmis wt tH20. 2Co3 бefer) ( actas Attdre Hoenayntut elaass оxnyn otions И6 нt Hieas Haamogh bn Lamys OLtgm product Ceu mehbalrsm фomd f Coz and Haeuhbis act as buber aud more to Ru yelaan Lab Manual

molecles «y*^ ikeujp fo frat it Ca a Moreto ^men acthe olapauH wiu relae its due fo ah and pickuys hekdnie rerdues rotansHeim) enly biar berat buffer more onyns band Lng aciln to FO. for ogng ph is loved Iu Solutan mne ack') o h02 ne ho6icabeuode) fom, butfe/ Lab Manual