I was surprised and impressed by the dramatic improvement observed in a Coombs-positive hemolytic anemia patient reported by Kuo et al (June 2001).1This outstanding result seems to have resulted from the fact that haptoglobin functioned properly, thanks to the healthy liver, which minimized damage to the kidneys and other organs caused by the onset of anemia. However, we may not always achieve such successful results. In order to make a decision on whether or not to conduct the blood transfusion, it is important that anemia-induced hemoglobin loads to kidneys and other organs are correctly evaluated. Haptoglobin, which is produced mainly in the liver, combines with hemoglobin produced as a result of hemolysis. This haptoglobin-hemoglobin complex is then taken into the liver and metabolized there. However, the amount of haptoglobin produced is often not enough to keep up with excessive hemolysis. As a result, a state of ahaptoglobinemia is induced, as in this clinical case. Moreover, when excessive hemoglobin amounts continue to be released, the haptoglobin elimination mechanism cannot keep up and, eventually, another metabolic route begins functioning. In other words, hemes are removed from excessive hemoglobin to become methemes and combined with albumin to form methemalbumin, which is metabolized in the liver. In view of this metabolic flow, detecting haptoglobin/metheme is exceedingly useful in detecting the level of hemoglobin load in anemia patients. The detection of both haptoglobin and methemalbumin fractions in the serum from patients was conducted using 5% polyacrylamide gel electrophoresis and o-dianisidine staining method (Figure 1
). The metheme concentration is directly proportional to the staining level of methemalbumin.2 This method allows simultaneous evaluation of both haptoglobin and metheme. Disappearance of haptoglobin and increase of metheme indicates extremely serious anemia. Detection of haptoglobin and methemalbumin contributes useful information for continued hemolysis follow-up.