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Biophysics of hemoglobin in chronic renal failure
New Egyptian Journal of Medicine [The]. 1996; 15 (1): 99-104
in English | IMEMR | ID: emr-42759
ABSTRACT
The imbalance in acid-base buffer capacities of Hb prior to dialysis is due to the unfolding of Hb as a globular protein. The new groups which by unfolding become exposed to its surface could be responsible for H+ and OH+ receptors. The drop in heme-heme interaction b and indicated a low affinity of Hb to oxygen. This signify the adaptation of macromolecule to deliver oxygen to the tissue. This adaptation is lost post-dialysis due to the rapid shift from acidosis to alkalosis. Thus, Hb is folded after being unfolded pre-dialysis. However, a slight decrease in Met-Hb and sulf-hemoglobin content was detected with corresponding elevation of tetramer Hb
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Index: IMEMR (Eastern Mediterranean) Main subject: Biophysics / Buffers / Hemoglobins Limits: Humans Language: English Journal: New Egypt. J. Med. Year: 1996

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Index: IMEMR (Eastern Mediterranean) Main subject: Biophysics / Buffers / Hemoglobins Limits: Humans Language: English Journal: New Egypt. J. Med. Year: 1996