Literature DB >> 8471844

One-step chromatographic method for the purification of avian serotransferrin.

A V Vieira1, W J Schneider.   

Abstract

Existing purification procedures for serum transferrins involve multistep chromatographic separations and require several days to complete. In addition, they have not been tested for purification of transferrins directly from the blood of egg-laying animals, where large amounts of circulatory lipoproteins can interfere with standard chromatographic separations. We have developed a procedure for purifying transferrin in one step directly from the serum of ovulating chickens. The method, which is based on hydrophobic interaction chromatography, gives a yield of about 12 mg (80%) of purified serotransferrin from 3 ml of serum and can be completed in a few hours.

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Year:  1993        PMID: 8471844     DOI: 10.1006/prep.1993.1016

Source DB:  PubMed          Journal:  Protein Expr Purif        ISSN: 1046-5928            Impact factor:   1.650


  2 in total

1.  High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization.

Authors:  S A Ali; H C Joao; R Csonga; F Hammerschmid; A Steinkasserer
Journal:  Biochem J       Date:  1996-10-01       Impact factor: 3.857

2.  Iron starvation of Bordetella avium stimulates expression of five outer membrane proteins and regulates a gene involved in acquiring iron from serum.

Authors:  T D Connell; A Dickenson; A J Martone; K T Militello; M J Filiatraut; M L Hayman; J Pitula
Journal:  Infect Immun       Date:  1998-08       Impact factor: 3.441

  2 in total

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