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PMID: 4038272 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

Comparison of human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass, isoelectric point, iron-binding properties and uptake by the liver.

The Biochemical journal ·Vol. 229 ·No. 2 ·1985-07-15 ·Pages 353-9

Moguilevsky N, Retegui LA, Masson PL

Abstract

Human lactoferrins isolated from neutrophilic leucocytes and milk by CM-Sephadex chromatography were similar in Mr (76000) and pI (8.7). Upon acidification, both proteins released their two Fe3+ ions/molecule in a similar biphasic way. Both proteins intravenously injected into mice were cleared from plasma at the same rate. The maximal uptakes by the liver, which occurred 5 min after injection, were inhibited to the same extent by milk lactoferrin used as a competitor.

MeSH Terms

Animals Electrophoresis, Polyacrylamide Gel Humans Iron/metabolism Isoelectric Point Lactoferrin/isolation & purification,metabolism Lactoglobulins/metabolism Liver/metabolism Macromolecular Substances Mice Mice, Inbred BALB C Milk/analysis Molecular Weight Neutrophils/analysis

Chemicals

Lactoglobulins Macromolecular Substances Iron Lactoferrin

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Moguilevsky N

Retegui L A

Masson P L

References (27)

27 references, click to expand

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Article Info

Journal

The Biochemical journal

Abbr.

Biochem J

ISSN

0264-6021

DOI

10.1042/bj2290353

Published

1985-07-15

Pages

353-9

Language

English

Region

England

NLM ID

2984726R

PMCID

PMC1145067

Subset

External Links

PubMed source DOI: 10.1042/bj2290353 PMC Full Text View journal details

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Comparison of human lactoferrins from milk and neutrophilic leucocytes. Relative molecular mass, isoelectric point, iron-binding properties and uptake by the liver.

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