Literature DB >> 2592487

Separation of the human transferrin isoforms by carrier-free high-performance zone electrophoresis and isoelectric focusing.

F Kilàr1, S Hjertén.   

Abstract

Human transferrin isoforms, i.e., molecules with different carbohydrate contents which differ from each other by only one negative charge, were resolved by high-performance zone electrophoresis in free solution. The di-, tri-, tetra-, penta-, hexa- and heptasialo transferrins could be assigned in the electrophoretic pattern. The pattern changed when iron-free transferrin was treated with neuraminidase, which splits off the sialic acid from the carbohydrate chains. The final digest contained transferrin molecules without sialic acids, as was confirmed by isoelectric focusing.

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Year:  1989        PMID: 2592487     DOI: 10.1016/s0021-9673(01)84304-1

Source DB:  PubMed          Journal:  J Chromatogr


  2 in total

1.  Preparation and investigation of bioactive transferrin-iron complexes formed with different synergistic anions.

Authors:  Judit Gálicza; Andrea Vargová; Viktor Sándor; Csongor Kálmán Orbán; Csaba Dezso András; Beáta Abrahám; Szabolcs Lányi; Ferenc Kilár
Journal:  Protein J       Date:  2012-01       Impact factor: 2.371

2.  Separation and analysis of the glycoform populations of ribonuclease B using capillary electrophoresis.

Authors:  P M Rudd; I G Scragg; E Coghill; R A Dwek
Journal:  Glycoconj J       Date:  1992-04       Impact factor: 2.916

  2 in total

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