Spectral Absorption Characteristics of Human Methemalbumin

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Abstract
Methemalbumin, an intermediary metabolite of intravascular hemoglobin catabolism, was made from purified human albumin and hematin and the synthetic material purified by DEAE Sephadex chromatography. The methemalbumin from paroxysmal nocturnal hemo-globinuria serum was separated by Pevikon block electrophoresis. Studies of the spectral absorption characteristics of both the chemically prepared and electrophoretically separated methemalbumin identified and confirmed the purity of these preparations. Four criteria were used for the detection of methemalbumin characteristic absorption spectrum with maxima at 623, 540, 500 and 403 m[mu]; a positive Schumm test; a positive dithionite test; and appropriate electrophoretic mobility of the benzidine positive band. Contrary to previous studies, it was shown that the addition of cyanide solution (5%) abolished th 625 m[mu] maximum of methemalbumin. Studies suggest that the previously reported resistance of methemalbumin to cyanide is incorrect and therefore can not be used as a basis for detecting this substance. In hemolytic serum there appears to be another substance, not methemalbumin, whose 628 m/x maximum resists alteration by cyanide. The nature of this substance is presently unknown.

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