Literature DB >> 3219132

[Fractionation of chicken egg glycoproteins and their purification using preparative HPLC].

V E Piskarev, E L Galenko, L M Likhosherstov, V A Derevitskaia, N K Kochetkov.   

Abstract

A new method of fractionation of hen egg glycoproteins has been developed. The procedure involves high-speed mass ion-exchange chromatography on ZetaPrep cartridges, differential precipitation, and ultrafiltration on "Minitan" tangential-flow system. Six fractions were obtained from egg white (ovomucin, avidin, riboflavin-binding glycoprotein RF-GPw, ovoinhibitor, ovalbumin-ovotransferrin, and ovomucoid fractions), and two fractions from egg yolk (riboflavin-binding glycoprotein RF-GPy and phosvitin fractions). Using ion-exchange HPLC on columns (150 X 21.5 mm) Protein PAK DEAE-5PW and SP-5PW, six homogenous glycoproteins (avidin, RF-GPw, ovalbumin, ovotransferrin, ovomucoid, and RF-GPy) were isolated in preparative quantities (0.1-1 g). Ion-exchange HPLC also resolves some glycoproteins' isoforms with different pI values.

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Year:  1988        PMID: 3219132

Source DB:  PubMed          Journal:  Bioorg Khim        ISSN: 0132-3423


  2 in total

1.  A novel preparative method for the isolation of avidin and riboflavin-binding glycoprotein from chicken egg-white by the use of high-performance liquid chromatography.

Authors:  V E Piskarev; A M Shuster; A G Gabibov; A G Rabinkov
Journal:  Biochem J       Date:  1990-01-01       Impact factor: 3.857

2.  Interaction of egg-white glycoproteins and their oligosaccharides with the monomer and the hexamer of chicken liver lectin. A multivalent oligosaccharide-combining site exists within the carbohydrate-recognition domain.

Authors:  V E Piskarev; J Navrátil; H Karásková; K Bezouska; J Kocourek
Journal:  Biochem J       Date:  1990-09-15       Impact factor: 3.857

  2 in total

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