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Hemoglobin Zürich. II. Physicochemical Properties of the Abnormal Hemoglobin

  • BACHMANN, FEDOR Department of Internal Medicine, University of Zürich, Switzerland. At present: Trainee (NIH), Department of Internal Medicine, Washington University, St. Louis, Mo.
  • MARTI, HANS R. Medical Out-patient Service, University of Basle, Switzerland.
Published in:
  • Blood. - American Society of Hematology. - 1962, vol. 20, no. 3, p. 272-286
Immunology
Cell Biology
Biochemistry
Hematology
English Abstract
The physicochemical properties of Hgb Zürich were investigated. This new hemoglobin is characterized by an electrophoretic mobility between Hgb A and Hgb S at pH 8.6. Similarly it runs between Hgb A and Hgb S on amberlite IRC 50 and on carboxymethylcellulose chromatography. Fingerprints of the tryptic digests revealed three unusual peptides; their existence may be explained by the replacement of one histidyl group by an arginyl group in peptides 20, 21 of the β-chain. At 70 C. Hgb Zürich is destroyed three times faster than Hgb A. The erythrocytes and hemolysates of Hgb Zürich carriers show an increased tendency to form methemoglobin. When incubated with acetylphenylhydrazine, the erythrocytes behave like glucose-6-phosphate dehydrogenase-deficient red cells. Carriers of Hgb Zürich tend to develop severe hemolysis after the ingestion of primaquine and a variety of sulfonamides. Glucose-6-phosphate dehydrogenase activity, glutathione stability and methemoglobin reduction tests have been found normal.
Language
  • English
Open access status
bronze
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Persistent URL
https://sonar.rero.ch/global/documents/193358
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