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Difference in Hemoglobin-Binding Ability of Polymers Among Haptoglobin Phenotypes

¹ Dept. of Forensic Sci., School of Allied Health Sci., Kitasato Univ., 1-15-1 Kitasato, Sagamihara City, 228 Japan ,
² Dept. of Biochem., Mitsubishi Kagaku Bio-Clin. Labs., Inc., Shimura 3-30-1, Itabashi-ku, Tokyo, 174 Japan

To the Editor:

Langlois and Delanghe (1) described several functional differences between haptoglobin phenotypes in this journal. They reviewed the functional properties of haptoglobin phenotypes such as ability for hemoglobin (Hb) binding, antioxidative capacity, and inhibition of prostaglandin synthesis, which were strong in Hp-1, intermediate in Hp2–1, and weak in Hp2–2. However, we do not agree with their results about the ability for Hb binding.

Hp2–1 and Hp2–2 phenotypes form many polymers, and analysis of the functional properties of each of the isolated polymer proteins had been very difficult (2). We designed new analytical methods such as crossed Hb electrophoresis (3) and two-dimensional affinity electrophoresis, using Hb (4) to identify the Hb-binding ability of each of the haptoglobin polymer proteins of Hp2–1 and Hp2–2 phenotypes. From the results of crossed Hb electrophoresis, we found that a haptoglobin molecule combined with equimolar amounts of Hb to form at least a hexamer. We confirmed by two-dimensional affinity electrophoresis that the larger polymer of the Hp2–2 phenotype had a lower affinity to Hb, but a . . . [Full Text of this Article]

Footnotes

References

Joris R. Delanghe and Michel R. Langlois

Dept. of Clin. Chem., University Hosp. Gent, De Pintelaan 185, B 9000 Gent, Belgium
^a Author for correspondence.

To the Editor:

References

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