Characterization of the Protein and Glycan Moieties in Different Forms of Bovine Lactoferrin

Ye, Xiuyun; Nishimura, Toshihide; Yoshida, Shigeru

doi:10.1271/bbb.61.782

Cited by 12 publications

(8 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In order to precisely determine the mass of lactoferrin, intact protein analysis using MALDI TOF MS (Figure A) in linear mode, was performed. Average masses of lactoferrin were in range of 77.167–81.189 kDa, which is in accordance with literature values (average mass range of 77–84 kDa , ). Differences in the masses are associated with the most common form of co- and post- translation protein modification: glycolysiation.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Silver-Lactoferrin Nanocomplexes as a Potent Antimicrobial Agent

et al. 2016

View full text Add to dashboard Cite

The process of silver immobilization onto and/or into bovine lactoferrin (LTF), the physicochemical properties of bovine lactoferrin and obtained silver-lactoferrin complexes, as well as antibacterial activity of silver-lactoferrin complexes were investigated in this work. Kinetic study of the silver immobilization into lactoferrin was carried out using batch sorption techniques. Spectrometric (MALDI-TOF/TOF-MS, ICP-MS), spectroscopic (FTIR, SERS), electron microscopic (TEM) and electrophoretic (I-DE) techniques, as well as zeta potential measurements, were applied for characterization of LTF and binding nature of silver in Ag-LTF complexes. On the basis of the results of the kinetics study, it was established that the silver binding to LTF is a heterogeneous process involving two main stages: (i) internal diffusion and sorption onto external surface of lactoferrin globules; and (ii) internal diffusion and binding into lactoferrin globule structure. Spectroscopic techniques combined with TEM analysis confirmed the binding process. Molecular dynamics (MD) analysis was carried out in order to simulate the mechanism of the binding process, and locate potential binding sites, as well as complement the experimental findings. Quantum mechanics (QM) simulations were performed utilizing density functional theory (DFT) in order to support the reduction mechanism of silver ions to elemental silver. Antimicrobial activity of synthesized lactoferrin complexes against selected clinical bacteria was confirmed using flow cytometry and antibiograms.

show abstract

Section: Resultsmentioning

confidence: 99%

“…Differences in the masses are associated with the most common form of co- and post- translation protein modification: glycolysiation. Studies have shown , that lactoferrin exhibits a degree of glycosylation changes and is associated, i.e., with stage of lactation, inflammation, environmental and stress conditions.…”

Section: Resultsmentioning

confidence: 99%

Silver-Lactoferrin Nanocomplexes as a Potent Antimicrobial Agent

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Further studies on milk have elucidated the occurrence of two bLf variants, bLf-a and bLf-b (Tsuji, Hirata and Matsuoka 1989), which arise as a result of different glycosylation patterns (Ye, Nishimura and Yoshida 1997;Wei, Nishimura and Yoshida 2000). The mass of bLf-a, at 84 kDa, is higher mass than that of bLf-b, at 81 kDa (Wei, Nishimura and Yoshida 2000;van Veen et al 2004).…”

Section: Glycosylation Sites Of Human and Bovine Lactoferrinmentioning

confidence: 99%

The N-glycans of lactoferrin: more than just a sweet decoration

Zlatina

Galuska

2021

Biochem. Cell Biol.

View full text Add to dashboard Cite

Nearly all extracellular proteins undergo posttranslational modification with sugar chains during their transit through the endoplasmic reticulum and the Golgi apparatus. These “sweet” modifications not only influence the activity of its carrier protein, but they themselves often have bioactivity, independent of the carrier function. Lactoferrin belongs to the group of glycoproteins and is modified with several different N-glycans. This review summarizes several studies dealing with the diverse glycosylation patterns of lactoferrin from different origins and the potential impact of these posttranslational modifications on the functionality of lactoferrin. A special emphasis is placed on the differences between human and bovine lactoferrin, since the latter form is often selected for the development of novel therapeutic approaches in humans. For this reason, the potential impact of the bovine-specific glycosylation patterns on the observed heterogeneous effects of lactoferrin in humans is discussed within this review.

show abstract

“…Although the structural differences between bovine milk and neutrophil lactoferrin glycans have not been determined to the same extent as for human lactoferrin, it seems clear that the situation is entirely analogous, and that functional differences between the two proteins are unlikely to occur. Indeed, bovine milk lactoferrin is itself heterogeneous, with two major forms having been identified, lactoferrin a and b, that differ in their glycosylation, but not in their polypeptide chains (Tsuji et al, 1989;Ye et al, 1997).…”

Section: Comparison Of Milk and Neutrophil Lactoferrinmentioning

confidence: 99%