Physical characteristics and polymerization during iron saturation of lactoferrin, a myelopoietic regulatory molecule with suppressor activity

C. Mantel, K. Miyazawa, Hal Broxmeyer

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24 Citations (Scopus)

Abstract

Lactoferrin (LF) has been implicated in normal regulation of myeloid blood cell production in vitro and in vivo and abnormalities in LF-cell interactions have been associated with progression of leukemia and other hematopoietic disorders. LF may be clinically useful and for this reason we studied selected biochemical characteristics of LF. Purified human milk LF was saturated with iron from solution and analyzed by gel electrophoresis, ion-exchange and gel filtration chromatography. The metalloprotein was found to contain several molecular weight species on polyacrylamide gels. High resolution ion-exchange chromatography demonstrated the binding of LF to both anionic and cationic media under identical conditions indicating a bipolar charge distribution. Gel filtration studies revealed a tetramerized form of LF, the formation and stability of which was dependent on the ionic strength of the solution.

Original languageEnglish
Pages (from-to)121-132
Number of pages12
JournalAdvances in Experimental Medicine and Biology
Volume357
StatePublished - 1994

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Lactoferrin
Polymerization
Iron
Molecules
Gels
Chromatography
Gel Chromatography
Ion exchange
Metalloproteins
Ion Exchange
Charge distribution
Ion Exchange Chromatography
Human Milk
Myeloid Cells
Ionic strength
Electrophoresis
Cell Communication
Osmolar Concentration
Blood Cells
Leukemia

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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AU - Broxmeyer, Hal

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AB - Lactoferrin (LF) has been implicated in normal regulation of myeloid blood cell production in vitro and in vivo and abnormalities in LF-cell interactions have been associated with progression of leukemia and other hematopoietic disorders. LF may be clinically useful and for this reason we studied selected biochemical characteristics of LF. Purified human milk LF was saturated with iron from solution and analyzed by gel electrophoresis, ion-exchange and gel filtration chromatography. The metalloprotein was found to contain several molecular weight species on polyacrylamide gels. High resolution ion-exchange chromatography demonstrated the binding of LF to both anionic and cationic media under identical conditions indicating a bipolar charge distribution. Gel filtration studies revealed a tetramerized form of LF, the formation and stability of which was dependent on the ionic strength of the solution.

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