Literature DB >> 3802549

Extended application of RP-HPLC for characterization of human hemoglobin variants.

V Baudin, H Wajcman.   

Abstract

The different steps for the structural study of a human hemoglobin, from protein isolation to amino acid analysis, can be achieved using as the only method reversed phase high performance liquid chromatography. HPLC allows effective and rapid separations on microquantities of material. The miniaturization of the techniques led to a new approach involving successive enzymic hydrolysis of peptides.

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Year:  1987        PMID: 3802549     DOI: 10.1016/0009-8981(87)90235-x

Source DB:  PubMed          Journal:  Clin Chim Acta        ISSN: 0009-8981            Impact factor:   3.786


  3 in total

1.  Improvement of oxygen-carrying properties of human hemoglobin by chemical modification with a benzene hexacarboxylate-monosubstituted polyoxyethylene.

Authors:  E Dellacherie; M Léonard
Journal:  J Protein Chem       Date:  1991-02

2.  Seventh International Conference on Methods in Protein Sequence Analysis. July 3-8, 1988, West Berlin, F.R.G. Short communications.

Authors: 
Journal:  J Protein Chem       Date:  1988-06

3.  Two new human hemoglobin variants caused by unusual mutational events: Hb Zaïre contains a five residue repetition within the alpha-chain and Hb Duino has two residues substituted in the beta-chain.

Authors:  H Wajcman; Y Blouquit; C Vasseur; A Le Querrec; M Laniece; C Melevendi; A Rasore; F Galacteros
Journal:  Hum Genet       Date:  1992-08       Impact factor: 4.132

  3 in total

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