Measuring relative rates of hemoglobin oxidation and denaturation.

摘要: Publisher Summary In aqueous media, without the active methemoglobin reductase system present in intact red blood cells, ferrous heme groups of hemoglobin can auto-oxidize to form continually increasing amounts high-spin ferric heme. Under conditions that promote tetramer dissociation, subsequent tertiary structural distortions globin monomers occur; these are associated with iron spin-state transitions and possible geometric moiety within individual pockets. Binding low-spin at sixth coordinate position normally distant amino acid side chains pocket then result formation accumulation soluble insoluble hemichromes. This chapter presents a generalized outline this pathway. An alternate degradative path is also shown, wherein transferred human serum albumin methemalbumin. The apoprotein thus formed insoluble.