Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility

Hekman, Annemarie

doi:10.1016/0005-2795(71)90126-7

Cited by 103 publications

(40 citation statements)

References 10 publications

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“…Addition of lactoferrin to lacrimal fluid affected its immunoelectrophoretic pattern. It bound serum albumin and IgA, and the mobility of the resulting complex was intermediary between those of the component proteins, which confirmed earlier results ob tained with isolated proteins | Hekman, 1971], By means of dodecyl sul fate gel electrophoresis it was established that the molecular weight amounted to 82,000, the same value found for lactoferrin from other sources and for transferrin [Aisen and Leibman, 1972], Lactoferrin has strong metal-binding properties and it is assumed that owing to this activity it inhibits the growth of certain microorganisms.…”

supporting

confidence: 79%

Lactoferrin and the Protective Function of the Lacrimal Fluid

Broekhuyse¹

1976

Ophthalmologica

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supporting

confidence: 79%

Lactoferrin and the Protective Function of the Lacrimal Fluid

Broekhuyse¹

1976

Ophthalmologica

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“…Lactoferrin would perhaps promote the formation of CCP lesions since this protein is known to associate strongly with acidic macromolecules to form complexes (8).…”

Section: Discussionmentioning

confidence: 99%

Lactoferrin in Human Pancreas

Colomb¹,

Pianetta²,

Estevenon³

et al. 1976

Digestion

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The protein composition of normal human pancreatic juice and pancreatic juice of men with chronic calcifying pancreatitis (CCP) were compared using immunodiffusion techniques. An additional protein was found in pathological pancreatic juice and this protein has been identified as lactoferrin. Its concentration has been determined. The indirect immunofluorescence method was used to detect and localize lactoferrin in 9 samples of human pancreas from 3 patients with CCP and 6 patients without CCP. The fluorescence was found in all samples. Lactoferrin staining was localized in lumen acinar and in the cytoplasm of the acinar cells. The fluorescence was stronger in the apical zone of acinar cells. When lactoferrin antiserum was incubated with lactoferrin insolubilized by glutaraldehyde, no fluorescence staining was detected. The differences between our results obtained by immunodiffusion and immunofluorescence techniques are explained by the different sensitivity of the two techniques and these results indicate that lactoferrin is a protein of pancreatic secretion.

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“…Further experiments with carbamylated FeLf and NANA-free FeLf revealed the importance of the electric charge of the protein for its binding to MPC. It is known that Lf tends to form complexes with many acidic molecules such as agaropectin, trypan blue (26), and albumin (27). Hence, the high isoelectric point (pI = 9.0) of Lf (21) could in part account for the reaction of FeLf with MPC.…”

Section: Comparison Of the Binding Of Felf To Various Mouse Cells ~2mentioning

confidence: 99%

The binding of human lactoferrin to mouse peritoneal cells.

Snick¹,

Masson²

1976

The Journal of Experimental Medicine

146

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Human iron-saturated Lf (FeLf), which was labeled with 125I or 50Fe, was found to combine with the membrane of mouse peritoneal cells (MPC) which consisted of 70% macrophages. The following experimental data suggested the involvement of a specific receptor. (a) The binding of FeLf to MPC reached a saturation point. (b) The binding of radioactive FeLf was inhibited by preincubating the cells with cold FeLf but not with human Tf, human aggregated and nonaggregated IgG, or beef heart cytochrome c (c) Succinylation and carbamylation of FeLf resulted in a loss of its inhibiting activity on the binding of radioactive FeLf. Removal of neuraminic acid from FeLf increased its inhibitory activity. (d) The ability of apoLf to inhibit the binding of FeLf to MPC was significantly lower than that of FeLf. The existence of a Lf receptor capable of concentrating Lf released from neutrophils on the membrane of macrophages could explain the apparent blockade of the release of iron from the reticuloendothelial system, which accounts for the hyposideremia of inflammation. A receptor for FeLf was also found on mouse peritoneal lymphocytes. The affinity constant of FeLf for both lymphocytes and macrophages was 0.9 X 12(6) liter/mol. Howerver, macrophages bound three times more FeLf molecules (20 X 10(6)) per cell than did lymphocytes (7 X 10(6)).

show abstract

Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility

Cited by 103 publications

References 10 publications

Lactoferrin and the Protective Function of the Lacrimal Fluid

Lactoferrin and the Protective Function of the Lacrimal Fluid

Lactoferrin in Human Pancreas

The binding of human lactoferrin to mouse peritoneal cells.

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