OVOTRANSFERRIN, also called conalbumin, is a glycoprotein with a molecular weight of 76,000. OVOTRANSFERRIN comprises approximately 13% of the protein content of egg albumen. More than sixty years ago, researchers determined that OVOTRANSFERRIN is an iron-binding protein, making the iron in a bacterial culture medium nutritionally unavailable to potentially harmful micro-organisms, such as Schigella dysenteria (for which iron is an essential nutrient).
These same investigators later determined that a fraction of human blood serum exerts the same iron-binding action as OVOTRANSFERRIN. This blood serum protein was initially named siderophilin, but today is known as human transferrin. OVOTRANSFERRIN and blood transferrin are now known to have similar amino acid compositions (see table), as well as similar carbohydrate content.
Table: Comparison of Amino Acids Profiles
Bovine Serum Transferrin
Advantages & benefits
As one of the largest manufacturers and suppliers worldwide of egg white proteins, Bioseutica®’s advanced extraction and purification processes yield products that are consistently chosen over other competitive products. All extraction and refining are done under cGMP guidelines for active pharmaceutical ingredients (API).
An important advantage of using Bioseutica®’s OVOTRANSFERRIN is the elimination of the risk of disease associated with bovine and human-derived transferrins.
Among the several protective functions of OVOTRANSFERRIN, the most important one is likely to be the antibacterial activity, which is directly related to the OVOTRANSFERRIN's ability to bind iron (Fe3+), making it unavailable for bacterial growth. This bacteriostatic activity can be enhanced by adding carbonate ion which is one of the iron ligands in the OVOTRANSFERRIN metal-binding site increasing the pH from 6 to 8 and immobilizing OVOTRANSFERRIN by covalent linkage to Sepharose 4B . An increase of the bacteriostatic activity towards E. coli O157:H7 as iron chelator was demonstrated using a combination of ovotransferrin, NaHCO3, and EDTA.
OVOTRANSFERRIN shows a protective function similar to those already ascertained for the homologous mammalian lactoferrin. These additional functions, in many cases not directly related to iron binding, are also displayed by the peptides derived from partial hydrolysis of ovotransferrin. Several defensive properties of OVOTRANSFERRIN are also possessed by its proteolytic fragments, these properties may be of importance for human wellness and its derivatives as dietary additives in normal and pathological human conditions.(1)
Transferrins have been identified as a required media ingredient for the maturation of cells. The role of transferrins in culture systems is to provide iron to cells and to detoxify the media by binding contaminating metal ions, such as zinc, iron, and aluminium in their di and trivalent forms.
OVOTRANSFERRIN (OTRF, also referred to as conalbumin) and OTRF-derived peptides, including IRW, IQW, and KVREGT, are, by virtue of their anti-inflammatory and antioxidant characteristics, viable treatment agents for endothelial dysfunction and the prevention of CVD (2).
In spite of the numerous discoveries of new anticancer drugs that work on different intracellular targets, many of these drugs have a considerable drawback as they are nonselective thus causing adverse side effects on normal cells. A new study is aimed to explore the potential of ovotransferrin (OTf) as a carrier molecule to allow specific targeting of anticancer drugs to cancer cells via the transferrin receptor (TfR). Receptor binding assay provided evidence that OTf bind to the transferrin-receptor (TfR) of human colon cancer cells. Two anticancer drugs, carboplatin (cbp) and paclitaxel (PTX) were non-covalently conjugated with OTf, at different mole ratios, through freeze-condensation. The two OTf conjugates showed superior anti-proliferative activities against human colon carcinoma (HCT-116) and human breast carcinoma (MCF-7) cells compared to the activities of free drugs, with OTf-cbp being the most potent conjugate. The conjugates with low drug loading inhibited cell growth more efficient than the high drug-loaded conjugates. Fluorescence staining with acridine orange and propidium iodide showed that HCT-116 cells treated with OTfcbp or OTf-PTX exhibited red fluorescence, indicating that PI entered to the nuclei as the cell membrane lost its integrity. The red fluorescence was accompanied by chromatin condensation and fragmentation indicates apoptosis. The results demonstrate, for the first time, that OTf could be utilized to specifically target drugs via TfR-mediated endocytosis to cancer cells and will help to pave the way for clinical studies as a potential targeting molecule (3).
OVOTRANSFERRIN belongs to a group of proteins called metalloproteinases that have been found to induce the production of heat shock proteins (HSPs). Clinical trials with OVOTRANSFERRIN have found that it is able to induce HSPs in the skin, which provides protection against cold stress and other environmental factors. HSPs play a fundamental role in life-essential processes and are associated with many areas of biology and medicine. They are known to help cells disassemble and dispose of damaged proteins and to help in the making and transport of new proteins. The role of HSPs in the aging process is not yet clear. However, the ability of OVOTRANSFERRIN to induce HSP production suggests it can be effectively utilized in personal care skin creams and moisturizers.
OVOTRANSFERRIN, like serum transferrin, is also similar in structure and function to lactoferrin from milk. However, OVOTRANSFERRIN can be extracted in larger quantities and is suitable for use in therapeutic programs. The addition of OVOTRANSFERRIN to cow’s milk (which is generally low in transferrins) enhances its antibacterial property and makes it comparable to human milk.
Several researches demonstrated the potential of ovotransferrin as a functional food ingredient for bone health due to its role in promoting osteoblastic activity and inhibiting osteoclastic activity common in osteoporosis. Ovotransferrin inhibits osteoclast formation and differentiation by attenuating the activation of NF-κB and MAPK pathways.
1. Francesco Giansanti, Loris Leboffe, Francesco Angelucci, Giovanni Antonini - The Nutraceutical Properties of Ovotransferrin and Its Potential Utilization as a Functional Food | Publisher Site
2. Shuang Chen, Hongmei Jiang, Hanhui Peng, Xiaosong Wu, and Jun Fang - The Utility of Ovotransferrin and Ovotransferrin-Derived Peptides as Possible Candidates in the Clinical Treatment of Cardiovascular Diseases | Publisher Site
3. Hisham R Ibrahim, Daiichi Miyawaki, Takeshi Miyata - Ovotransferrin as a novel drug-targeting molecule for cancer chemotherapy | Publisher Site
4. Ethige Chathura Nishshanka Rathnapala, Dong Uk Ahn & Sandun Abeyrathne - Functional properties of ovotransferrin from chicken egg white and its derived peptides: a review | Publisher Site
5. Nan Shang and Jianping Wu - Egg White Ovotransferrin Attenuates RANKL-Induced Osteoclastogenesis and Bone Resorption | Publisher Site
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