Literature DB >> 11944920

Detection of a novel variant human hemoglobin by electrospray ionization mass spectrometry.

Heinz Troxler1, Frank Neuheiser, Peter Kleinert, Thomas Kuster, Claus W Heizmann, Ragna Sack, Peter Hunziker, Thomas J Neuhaus, Marlis Schmid, Hannes Frischknecht.   

Abstract

A novel hemoglobin variant was detected by electrospray ionization mass spectrometry. Hb Zurich-Hottingen is characterized by an Asn --> Ser replacement in the alpha-chain at position 9 as confirmed by DNA analysis. This hemoglobin variant is silent in isoelectric focusing, reversed-phase chromatography, and cation-exchange chromatography. The mutant alpha-chain was detectable only with electrospray mass spectrometry by its mass shift of -27 Da. The carrier was found to be heterozygous for the new hemoglobin variant. These results illustrate the power of ESI mass spectrometry for hemoglobin analysis. (c)2002 Elsevier Science (USA).

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Year:  2002        PMID: 11944920     DOI: 10.1006/bbrc.2002.6762

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Covalent modifications of hemoglobin by nitrite anion: formation kinetics and properties of nitrihemoglobin.

Authors:  Mai Otsuka; Sarah A Marks; Daniel E Winnica; Andrew A Amoscato; Linda L Pearce; Jim Peterson
Journal:  Chem Res Toxicol       Date:  2010-10-20       Impact factor: 3.739

2.  Mutations in the paralogous human alpha-globin genes yielding identical hemoglobin variants.

Authors:  Kamran Moradkhani; Claude Préhu; John Old; Shirley Henderson; Vera Balamitsa; Hong-Yuan Luo; Man-Chiu Poon; David H K Chui; Henri Wajcman; George P Patrinos
Journal:  Ann Hematol       Date:  2008-10-16       Impact factor: 3.673

  2 in total

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