Components of Healthy Grass-Fed Whey

April 18, 2011
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VITAL WHEY PROTEINS

Beneficial elements of non-denatured, grass-fed whey

The following are detailed descriptions of the benefits of 3 types of proteins that are found in all of Paleotrition’s whey protein shakes (our sponsor).  Unlike most commercial whey protein powders, our whey comes from healthy year-round grass-fed cows.  Because of this, we don’t need to “ultra pasteurize” it.  In other words, we don’t need to kill all the good stuff to kill the bad stuff – because milk from healthy cows doesn’t have any of the bad stuff. 

All of these proteins are highly beneficial to healthy people and to people with health issues.  They help our immune and digestive systems function properly. 

Immunoglobulins

Immunoglobulins are proteins produced by plasma cells of the bone marrow.  They play an essential role in the body’s immune system. They  act as antibodies in response to foreign substances that may potentially harm you such as bacteria, viruses, fungus, animal dander, or cancer cells. Immunoglobins are attached to these substances so the immune system can destroy them.

These naturally occurring proteins were discovered in 1890 and were used as supplements for domesticated animals, improving growth rates and appetite in stressed, immune-deficient animals (Kats et al., 1990), reducing morbidity (Gomez et al., 1998), improving lean tissue accretion and protein efficiency (Jiang et al., 2000), and functioning as a natural replacement for antibiotics as growth promotants (Coffey and Cromwell, 1995).

Coffey and Cromwell (2002) even published a review of 50 studies that had been conducted on immunoglobulins.  They proved beneficial in 89% of the studies. According to Kishimoto, C. (2007), based on 60 clinical studies made on the therapeutic effects of Immunoglobulin, the researchers found out that it does not only boost your immune system, but also helps improve the health of your gastrointestinal tract, promote a healthy inflammatory response, helps reduce cholesterol, and acts as a source of high quality protein for building lean body mass and recovering from exercise.

Several studies have shown reduced levels of immunoglobulins in various athletes (Garagioloa, et al. 1995; Gleeson et al. 1995). According to Jay Hoffman, author of the book entitled, “Physiological aspects of sport training and performance”, the reduced levels of immunoglobulins of both endurance and non-endurance athletes is likely caused by their intense exercise training. The lower these levels, the higher they are susceptible to infection.

Therefore, athletes and non-athletes can benefit from high quality protein because immunoglobulin boosts and strengthens the immune system, gets more amino acids into muscle cells throughout the body, promotes muscle tissue growth, regeneration, and strengthening, initiates the transport of nucleic acids into the cell nucleus, where the DNA resides, provides the raw material needed to repair damage to the DNA and initiate cell division, supports reduction of pro-inflammatory cytokines, helps in post-exercise recovery, and is beneficial in repairing extreme muscle rips.

 

Lactoferrin

Lactoferrin is an iron-binding glycoprotein that belongs to the transferrin family. It is found throughout the human body and occurs in all secretions that bathe mucous membranes like saliva, tears, bronchial and nasal secretions, hepatic bile, and even pancreatic fluids. Lactoferrin is the primary germ-fighting compound naturally occurring in breast milk (Richards, 2008).

According to John Hill, author of the book entitled “Natural Treatments for Genital Herpes, Cold Sores and Shingles”, the lactoferrin concentration in bovine (cows) milk is only 0.5% to 1.0% while human breast milk can contain as much as 15% lactoferrin.

Another book entitled “Advances in Lactoferrin Research” by Geneviève Spik says lactoferrin is known to exert bacteriostatic effects due to its ability to bind environmental iron to microbial membranes. Its biological functions include modulation of the inflammatory response, activation of the immune system, and control of myelopoiesis or cell growth.

Lactoferrin plays significant roles in human biology. First, lactoferrin is believed to be the primary or sole source of iron for breast fed infants. Second, it appears to have antibacterial, antiviral, antifungal, anti-inflammatory, antioxidant and immunomodulatory activities which are very beneficial to one’s health.

Several studies found that lactoferrin has “potent” anti-viral effects against replication of both human HIV and vytomegalovirus (CMV). It is a powerful anti-microbial that inhibits a wide range of gram positive and gram negative bacteria, yeasts, and even some intestinal parasites. It also acts as both iron binding agent and iron donor that scavenges free iron. It has a powerful anti-cancer agent that can suppress the growth of human pancreatic cancer cells.

 

Lactoferrin has a physiological role in bone growth, and considered as a potential therapeutic agent for bone disorders, such as osteoporosis, and might have utility as a local agent to promote bone repair (Naot, D., Grey, A., Reid, I., & Cornish, J., 2005).

 

From a couple of clinical trials made, research experts suggest oral lactoferrin as having dosage of 40 mg daily while those people using supplement with lactoferrin can usually take 250 mg daily. The dosage and administration of lactoferrin depends on the physiological needs of one’s body.

 

Serum Albumin

 

Serum Albumin is a protein found in liver that helps maintain the osmotic pressure between the blood vessels and tissues. It accounts for 55 percent of the total protein in blood plasma. It has primary functions such as to transport essential fatty acids from adipose tissue to muscle tissue. Albumin likewise contributes to the regulation of osmosis and helps transport hormones, drugs and other substances through the bloodstream.

 

Albumin is a major protein in the human body. It consists about 60% of total human plasma protein by mass. Many hormones, drugs, and other molecules are mostly bound to albumin in the bloodstream. They must be released before becoming biologically active (Walsh, 2001).

 

Karol Mathews (2008) states that this kind of protein is used for treating various conditions such as shock due to blood loss in the body, burns, low protein levels due to surgery or liver failure, and as an additional medicine in bypass surgery. It is a concentrate of plasma protein that works by increasing plasma volume or serum albumin levels.

 

In the pharmaceutical industry, serum albumin has important medical uses. It promotes human growth, detection, maturation, and maintaining osmotic pressure. It also acts as an active element that binds different drugs in the liver and carries it throughout the blood stream. Researchers found out that a decrease in serum albumin concentration’s in critical illness is known to be associated with hyperthyroidism, hypoalbuminemia, and edema (Anaesth, 2000).

 

 

References:

Hoffman, J. (2002). Physiological aspects of sport training and performance. Human Kinetics. pp. 66-67.

 

Immunoglobulins. Retrieved on April 15, 2011, from http://www.webmd.com/a-to-z-guides/immunoglobulins.

 

Cowan, R.A., Gaw, A., & Murphy, M.J. (2008). Clinical biochemistry: an illustrated colour text 4th Ed. Elsevier Limited. p. 50.

 

Kishimoto, C. (2007). Immunoglobulin Therapy, Myocardial Diseases and Atherosclerosis: Recent Experimental and Clinical Studies. Current Cardiology Reviews, 3, 15-2. Rettrieved on April 15, 2011, from http://www.benthamscience.com/ccr/sample/ccr3-1/D0003CR.pdf.

 

Katz, V.L., Thorp, J.M., Watson, WJ. el al. (1990). Human immunogloblin

therapy for preeclampsia associated with lupus anticoagulant and

anticardiolipin antibody. Obstet. GynecoL, 76, 986-988.

 

Gomez GG, Phillips O, Goforth RA. (1998). Effect of immunoglobulin source on survival, growth and hematological and immunological variables in pigs, J.  Anim. Sci., 76: 1-7.

 

Jiang, R., X. Chang, B. Stoll, K. J. Ellis, R. L. Shypailo, E. Weaver, J. Campbell, & Burrin, D. G. (2000). Dietary plasma protein is used more efficiently than extruded soy protein for lean tissue growth in early-weaned pigs. J. Nutr. 130: 2016-2019.

 

Coffey, R. D., and G. L. Cromwell. 1995. The impact of environment and antimicrobial agents on the growth response of early-weaned pigs to spray-dried porcine plasma. J. Anim. Sci. 73: 2532-2539.

 

Garagiola, U., M., Buzzetim, E., Cardella, F., Confalonieri, Giani, V., Polini, P.   Ferrante, R. Mancuso, M. Montanari, E. Grossi and A. Pecori (1995). Immunological patterns during regular intensive training in athletes: Quantification and evaluation of a preventive pharmacological approach. J. Inter. Medical Res., 23: 85-95.

 

Gleeson, M., A.W. Macdonald, D.B. Cripps, R.L. Pyne, Clancy and PA. Fricker, (1995). The Effect on Immunity of long term Intensive Training in Elite

Swimmers. Clinical and Experimental Immunology, 102: 210-216.

 

The Benefits of Immunoglobulins. Retrieved on April 15, 2011 from

http://ignitenaturals.com/articles/the-benefits-of-immunoglobulins/.

 

Hormone-Free Bovine Immunoglobulin Concentrate: Immune Boosting Protein. Retrieved on April 15, 2011 from http://living-well.net/2009/11/17/hormone-free-bovine-immunoglobulin-concentrate-immune-boosting-protein/.

 

INTRAVENOUS IMMUNE GLOBULIN. Retrieved on April 15, 2011, from http://hospitals.unitedbloodservices.org/hospitalnewsletters/December2003.pdf.

 

Spik, G. (1998). Advances in Lactoferrin Research (Advances in Experimental Medicine and Biology). Plenum Press, New York. pp.41.

 

Hill, J. (2008). Natural Treatments for Genital Herpes, Cold Sores and Shingles: 2nd Ed. Clear Springs Press. pp. 36-39.

 

 Richards, B. (2008). Lactoferrin – Keeping Candida Friendly. Retrieved on April 18, 2011, from http://www.wellnessresources.com/tips/articles/lactoferrin_ keeping_candida_friendly/.

 

Naot, D., Grey, A., Reid, I., & Cornish, J. (2005). Lactoferrin – A Novel Bone Growth Factor. Retrieved on April 18, 2011, from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1183439/.

 

Walsh, G. (2001). Proteins: Biotechnology and Biochemistry: 2nd Ed. Wiley Publisher. pp.230-232.

 

Mathews, K. (2008). The therapeutic use of 25% human serum albumin in critically ill dogs and cats. The Veterinary clinics of North America Small animal practice. 38(3). pp. 595-605. Retrieved on April 18, 2011, from http://www.mendeley.com/research/therapeutic-25-human-serum-albumin-critically-ill-dogs-cats/.

 

Anaesth, B. (2000). The role of albumin in critical illness. 85 (4): 599-610. Retrieved on April 18, 2011, from http://bja.oxfordjournals.org/content/85/4/599.full.

 

 

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