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ISSN electronic edition: 1336-9075
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Hemoglobin. XVI. The isolation and characterization of hemoglobin chains of the monkey Macacus rhesus

P. Mäsiar and J. Vnek

P. J. Šafárik University, Košice


Abstract: cf. CA 58, 11590c. From the cryst. hemoglobin of M. rhesus the globin was isolated and its structure studied by chromatographic and spectrophotometric methods. The globin was fractionated on the ion exchanger IRC50(X)E64. For the development of the chromatogram and the elution of the fractions 2-8M urea at pH 1.8 was applied. The hemoglobin is composed of 2 homologous chains, α and β. N-terminal amino acid residues of both chains are in full agreement with the ending of α and β chains of human hemoglobin. The similarity with the human hemoglobin was proven by the isolation and identification of high basic peptides contg. histidine, which are characteristic for α and β types of polypeptide chains of human hemoglobin.

Full paper in Portable Document Format: 175a346.pdf (in Slovak)


Chemical Papers 17 (5) 346–352 (1963)

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