Literature DB >> 1247589

Failure of rabbit reticulocytes to incorporate conalbumin or lactoferrin iron.

E J Zapolski, J V Princiotto.   

Abstract

Despite the remarkable molecular similarity of human lactoferrin and human transferrin, the results of this investigation indicate that human lactoferrin was unable to furnish rabbit reticulocytes with iron for heme synthesis. Although conalbumin closely resembles transferrin in many of its properties, conalbumin iron-binding differs from human transferrin iron-binding. There are conflicting reports in the literature regarding conalbumin's ability to furnish iron to reticulocytes. In this study, small amounts of lactoferrin or conalbumin were adsorbed to mature and immature cell surfaces but neither of these iron-binding proteins surrendered iron intracellularly to reticulocytes for heme synthesis.

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Year:  1976        PMID: 1247589     DOI: 10.1016/0304-4165(76)90171-9

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  4 in total

1.  Preferential utilization in vitro of iron bound to diferric transferrin by rabbit reticulocytes.

Authors:  E J Zapolski; J V Princiotto
Journal:  Biochem J       Date:  1977-08-15       Impact factor: 3.857

2.  Transferrin-receptor interaction and iron uptake by reticulocytes of vertebrate animals--a comparative study.

Authors:  B C Lim; H J McArdle; E H Morgan
Journal:  J Comp Physiol B       Date:  1987       Impact factor: 2.200

3.  Characterization of monoferric fragments obtained by tryptic cleavage of bovine transferrin.

Authors:  J H Brock; F R Arzabe; N E Richardson; E V Deverson
Journal:  Biochem J       Date:  1978-04-01       Impact factor: 3.857

4.  Uptake and handling of iron from transferrin, lactoferrin and immune complexes by a macrophage cell line.

Authors:  R Oria; X Alvarez-Hernández; J Licéaga; J H Brock
Journal:  Biochem J       Date:  1988-05-15       Impact factor: 3.857

  4 in total

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