FREE SHIPPING ON ALL ONLINE DOMESTIC ORDERS

0
  • 0 0

Bovine Immunoglobulins in the Immune System | OraMune

What is Bovine Immunoglobulin (Ig)?

Bovine Ig, immunoglobulin concentrate, is a revolutionary new protein source that is based on immunoglobulin derived from serum. It is the first new protein source to come to the protein market in many years. Unlike traditional sources of protein such as casein or whey, bovine Ig is rich in naturally occurring, bioactive proteins such as immunoglobulin and peptides. Proprietary separation and filtration technologies are used to concentrate the bioactive proteins (>85%), which are principally specialized glycoproteins called immunoglobulins(>50%), that are found in serum and serve to protect the body against infection among other roles in the body. The powerful functionality and bioactivity of the proteins and peptides goes beyond the nutritional benefits of an excellent amino acid profile to provide direct immune support, stronger gut barrier function, and protection against over activation of the immune system.

Is there science to support the use of bovine Ig in humans?

If the processing technology would have existed, this product should have been launched many years ago because the basic science behind the product is recognized in every immunology textbook. Bovine Ig is derived from serum. Serum has two well known characteristics that make it an ideal raw material source for a revolutionary new protein source: 1) Serum contains the humoral immune system. The humoral factors of serum are one of the body’s major defenses against infection; 2) Serum provides the critical factors and nutrients for protein synthesis. It is the gold standard of all natural substances in supporting cell growth, proliferation and wound healing. Cells thrive when the media is supplemented with bovine serum. The origin of the concept for bovine Ig is founded on proven efficacy in food animals. More than 50 studies have been published in animal sciences demonstrating that oral or dietary plasma or serum protein supplementation promotes growth1, particularly lean tissue growth, by both supporting gut barrier function2 and modulating the immune response3.

What ensure that bovine Ig is a safe product to use?

Bovine Ig consists of naturally occurring proteins that are concentrated using stringent quality control procedures. The raw material is collected in USDA-inspected facilities and approved for use in food products. The purification of the Ig takes place in a closed system, which prevents against contamination. The facility itself is compliant with FDA Good Manufacturing Practices (GMP) for food products. The final product must meet more stringent internal quality standards than the standards for ingredients used in infant formula. A long history of use in the food 3;16;17.supply, the presence of low concentrations of the primary proteins in milk, and published clinical studies in both adults4 and children support the safety of the product5;6.

What is the mode of action?

Bovine Ig, due to the consistent, high concentration of immunoglobulins and other bioactive proteins and peptides in plasma or serum, has been shown to boost immunity and increase lean tissue accretion in animal studies1;7-13. But, the most exciting aspect of the science is new studies that demonstrate a positive modulation of gut barrier function2;14; 15 and inflammatory cytokine production and expression3;16;17. The effects of bovine Ig on inflammatory cytokine production provides a partial explanation of how bioactive proteins have positive effects on both intestinal permeability and amino acid utilization9. Recent studies of the biological roles of cytokines have opened up a new opportunity towards maximizing protein retention and lean body mass18-25. In bovine Ig or other means to manage cytokines has great potential to reduce the loss of protein through catabolism that is initiated by overstimulation of the immune system.

How does bovine Ig compare to other proteins?

Like other high quality sources of animal proteins such as meat, milk, or eggs bovine Ig has an excellent amino acid profile. Bovine Ig also has a neutral taste, odor and excellent solubility. However bovine Ig stands alone as a source of proteins and peptides with biological activity and functionality14;30. No other protein source has bioactive immunoglobulins and peptides as its predominant protein component. So bovine Ig differs completely in purpose of use to other protein sources. Proteins like eggs albumin, casein and whey can be used as sole sources of dietary protein due to a highly available, balanced, essential amino acid profile but theses proteins have negligible bioactivity. Bovine Ig, on the other hand, is rich in bioactive proteins, which helps promote amino acid utilization9;11;13. Also, the proteins are relatively large and more complex in structure than whey or casein with a slower rate of digestion, which allows them to retain biological activity and provide amino acids to the body for a longer period of time. Bovine Ig can be combined with whey or other high quality protein sources lower in molecular weight with a more rapid rate of digestion to optimize protein utilization. Retaining biological activity is critical to the dual-benefit of promoting lean tissue growth and amino acid utilization while also supporting immunity. 6.

Is bovine Ig broken down by digestion?

Immunoglobulin, unlike most proteins, is not completely broken down by digestive processes, which helps it maintain it’s biological activity throughout the GI tract. IgG is stable in mildly acidic conditions (pH of 4) and is not easily hydrolyzed by digestive enzymes. A summary of studies in which the degradation of IgG was studied in various in vitro and in vivo conditions is available. Approximately 20-25% of the immunoglobulin administered survives digestion and degradation. The “survival” of immunoglobulin through the digestive process explains why mothers produce milk enriched with antibodies to protect the neonate, why adults produce and secrete large quantities of immunoglobulin into the digestive tract, and why supplementation has proven to be of benefit to humans and animals.

How should bovine Ig be used?

For best results, bovine Ig should be consumed in capsules, chewable tablets, protein powders, bars or beverages in a daily serving of 5-10g per day for adults (or 150mg in bovine Ig per kg BW in children) or a rate of 10% of the protein in the product. A level of 2.5 grams per day is recommended for daily immune support. IG is recommended for use in dietary supplements, protein supplements, medical foods and functional foods. The specific applications recommended are products designed for: immunity, gut health, anti-inflammatory products, pre- and post- workout supplements to support recovery; and, with its slow digestion characteristics, bovine Ig is an ideal supplemental protein source for meal replacement products in weight loss. Isoleuine and methionine are the limiting amino acids in bovine Ig. For best results, bovine Ig should be a part of a complete, balanced nutritional program.

REFERENCES:

  1. Manners DJ, Mason AJ, Patterson JC. The structure of a beta-(1-3)-glucan from yeast cell walls. Biochem. J. 135: 19-30, 1973.
  2. Williams DL, Sherwood ER, Browder JW, etal. Pre clinical safety evaluation of soluble glucan. Int. J. Immunopharmacol. 10: 405-411, 1988.
  3. DI Luzio NR. Pharmacology of the reticuloendothelial system: accent on glucan. In The Reticuloendothelial System in Health and Disease. Reichard S, Escobar M, and Friedman H, eds. New York, Plenum Press, pp 412-421, 1976.
  4. Wooles WR, DI Luzio NR, The phagocytic and proliferative response of reticuloendothelial system following glucan administration. J. Reticuloendothelial Sec. 1: 160, 1964.
  5. Czop LK, Kay j. Isolation and characterization of beta glucan receptors on human mononuclear phagocytes. J. Exp. Med. 173: 1511-1520, 1991.
  6. Taylor PR, Brown GD, Reid DM, Willment JA, etal. The beta-glucan receptor, Dectin-1 is predominantly expressed on the surface of cells of the monocyte/ macrophage and neutrophil lineages. J. Immunol. 169: 3876-3882, 2002.
  7. Brown GD, Taylor PR, Reid DM, Willment JA, etal. Dectin-1 is a major beta-glucan receptor on macrophages. J. Exp. Med. 196: 407-412, 2002.
  8. Herr J, Marshall AS, Caron E, Edwards AD, etal. Derctin-1 utilizes novel mechanisms for yeast phagocytosis in macrophages. Blood Aug 10 (pub ahead of print).
  9. Suzuki I, Tanaka H, Kinoshita A, Oikawa S, etal. Effect of orally administered beta-glucan on macrophage function in mice. Int. J. Immunopharmacol. 12:675-678, 1990.
  10. Kokoshis PL, Williams DL, Cook JA, Di Luzio NR. Increased resistance to Staphylococcus aureus infection and enhaucement in serum lysozyme activity by glucan. Science 24: 1340-1342, 1978.
  11. Di Luzio NR, Williams DL, McNamee RB, Malshet VG. Comparative evaluation of the tumor inhibitory and antibacterial activity of solubilized and particulate glucan. Recent results cancer res. 75: 165-72, 1980.
  12. Reynolds JA, Kastello MD, Harrington DG, Crabbs CL. Glucan-induced enhaucement of host resistance to selected infectious diseases. Infect. Immun. 30: 51-57, 1980.
  13. Williams DL, Sherwood ER, Brewder IW, Mcnamee RB, etal. Effect of glucan on neutrophil dynamics and immune function in Escherichia coli peritonitis. J. Surg. Res. 44: 54-61, 1988.
  14. Williams DL, Di Luzio NR. Glucan-Induced modification of murine Viral hepatitis. Science 208: 67-69, 1980.
  15. Bistoni F, Vecchiarelli A, Cenci E, puccetti P, etal. Evidence for macrophage-mediated protection against lethal Candida albicns infection. Infect. Immun. 51: 668-674, 1986.
  16. Williams DL, Cook JA, Hoffman EO, etal. Protective effect of glucan in experimentally induced candidiasis. J. Reticulocndothelial Soc. 23: 479-490, 1978.
  17. Di Luzio NR, McNamee R, Browder WI, Williams D. Glucan: Inhibition of tumor growth and enhancement of survival in four syngeneic murine tumor models. Cancel Treat. Rep. 62: 1857-1866, 1978.
  18. Di Luzio NR, Williams DL, McNamee RB, etal. Comparative tumor inhibitory and anti-bacterial activity of soluble and particulate glucan. Int. J. Cancer. 24: 773-779, 1979.
  19. Di Luzio NR, McNamee R, Jones E, etal. The employment of glucan and glucan activated macrophages in the enhancement of host resistance to malignancies in experimental animals. In M. D. Fink ed. The Macrophage in Neoplasia, pp. 181-198, Academic Press, New York 1976.
  20. Mansel PWA, etal. Macrophage-mediated destruction of human malignant cells in vivo. J. Natl. Cancer Inst. 54: 571-580, 1975.
  21. Stewart CC, etal. Preliminary observations on the effect of glucan in combination with radiation and chemotherapy in four murine tumors. Cancer Treat. Rep. 62: 1867-1872, 1978.
  22. Di Luzio NR, Cook JA, Cohen C, etal. Enhancement of the inhibitory effect of cyclophosphamide on experimental acute myclogenous leukemia by glucan immunopotentiation and the response of serum lysozyme. In control of Neoplasia by Modulation of the Immune System. Ed. M. Chigiros. New York, Raven press 1978.
  23. Sveinbjornsson B. Inhibition of extablishemtn and growth of mouse liver metastases after treatment with interferon gamma and bet-1,3-glucan. Hepatology 27: 1241-1248, 1998.
  24. Gyorgy A. Czop JK. Stimulation of human monocyte beta glucan receptors by glucan particies induces production of UNF alpha and IL-1 beta. J. Immunopharmac. 14:1363-1372, 1992.
  25. Patcheu MI., Mac Vittie TJ. Stimulation of hemopoiesis and euhanced survival following glucan treatment in sub lethally and lethally irradiated mice. Int J. Immunopharmacol. 7:923-923, 1985
  26. Patchen MI., D' Alesandro MM, Brook I, etal. Glucan: mechanisms involved in its "radio protective" effect. J. Leukoe Biol. 24:95-105, 1987.
  27. Patchen MI., MacVittie TJ, Brook I. Glucan-induced hemopoietic and immune stimulation: therapeutic effects in sub lethally and lethally irradiated mice. Methods Find. Exp. Chin, Pharmacol. 8:151-155, 1986.
  28. Walk M, Danon D. Promotion of wound healing by yeast glucan evaluated on single animals. Med Biol. 63:73-80, 1985.