Natures Life: Green Whey Pro-96® Protein 13oz

Green Whey Pro-96® Protein - 13oz



by   Natures Life
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UPC: 040647004450
# 15445


Product #: 445
Size: 442g
Directions: Mix 1 scoop or 5 tablespoons of Green Whey™ with 8 ounces of water or your favorite beverage for a nutritious vanilla bean shake that is sugar free and 100% natural. Store in a cool, dry place.

Serving Size: 5 tbsp
Ingredients: Amount per serving: % Daily Value: +
Calories 110 ~
Calories from Fat 7 1%
Total Fat <1 g 1%
Cholesterol 15 mg 5%
Sodium 123 mg 5%
Total Carbohydrate 12 g 4%
Dietary Fiber 3 g 12%
Sugar <1 g 0%
Sugar Alcohols 5 g ~
Protein 21 g 42%

Other Ingredients: Highly Purified 100% Isolate Protein from milk, Organic Vanilla Flavor with other Natural Flavors, Maltodextrin, Erythritol, Maltitol, Xylitol, Proprietary Blend of Super Greens (To 10 Raw Foods), Luo Han Guo (Fruit Extract), Bromelain from

WHEY PROTEINS

Features & Benefits

  • Good source of branched-chain amino acids (BCAAs), plus all essential amino acids

  • Improves muscle performance and body composition

  • Supports healthy antioxidant levels and promotes healthy immune function

  • Green-Whey Pro-96™ contains antioxidant carotenoids and flavonoids

  • Promotes normal cell growth and inhibits abnormal cell growth

  • Supports healthy blood pressure and normal cholesterol and triglyceride levels

Facts About Whey Protein:

Whey is a major protein in milk. Cheese making produces liquid whey as a by-product. Whey protein is comprised primarily of simple proteins called lactoglobulins. Whey also contains some serum (blood) globulins including alpha-globulin, beta-globulin, gamma-globulin and immunoglobulins, which are the primary immune-system-stimulating features of whey.

Other components of whey protein include: enzymes, minerals, iron binding proteins, and vitamins, including B-12.1 Whey transits the stomach quickly 2 and the nutrients are rapidly absorbed in the human intestine. Casein (another milk protein), on the other hand, leaves the stomach slowly since it tends to "clot" in the stomach.3 Humans digest whey more easily than casein because it’s more natural for us; human milk contains more whey than casein.

Whey protein, often referred to as lactalbumin, is currently a preferred protein source for many endurance and strength athletes, who may require over twice the current daily recommended protein intake.4,5 In one trial, a whey-based supplement given to men and women for three months increased muscle performance, while those taking a placebo saw no improvement.6 In a study of weight-loss using a low-calorie diet and strength training, adding whey protein to the diet resulted in similar weight loss but greater reductions in body fat while preserving lean body mass.7 Whey has been shown to promote growth in experimental animals, low birth-weight infants, and burn victims.8,9,10,11

BCAAs: Athletes who are undergoing, or have undergone, intense prolonged exercise receive much of their energy from branched-chain amino acids (BCAAs)—leucine, isoleucine, and valine. These amino acids are unique in their ability to provide a ready and direct energy source to skeletal muscle during endurance exercise.12 An adequate dietary supply of BCAAs is needed during exercise to prevent unwanted muscle breakdown, or catabolism, and to help maintain cells.13 Whey is considered to be an excellent source of BCAAs, as well as the important sulfur amino acids methionine and cysteine.

Antioxidants & Protein: Glutathione is a powerful antioxidant involved chiefly in liver detoxification. Research has indicated free-radical production normally results from the rise in oxygen consumption with exercise, and that glutathione levels can decrease with exercise.14,15 Some researchers think that an increased intake of antioxidants like glutathione might protect athletes against minor muscle injuries.16 Whey protein supplementation in humans has been shown to increase blood levels of glutathione.17

Enhancing glutathione and antioxidant function is one of many ways whey protein supports normal immune function; other mechanisms are just beginning to be understood.18,19,20 One beneficial effect of whey on immune function is its ability to directly inhibit potentially harmful gastrointestinal bacteria.21,22 Also, some whey proteins appear to be able to help regulate normal cell growth and prevent abnormal cell growth,23,24,25,26,27,28 and may be superior even to soy protein in these beneficial effects.29

New Benefits for Whey : Recent research has discovered components of whey protein that may support heart health by promoting proper blood pressure regulation 30,31,32,33 and by protecting the body from unhealthy forms of cholesterol.34 In a placebo-controlled study, beverages containing whey protein used by adult men for eight weeks promoted normal levels of blood pressure, blood triglycerides and HDL ("good") cholesterol.35

Maintaining healthy bones may also be a benefit of whey protein. Some whey components besides calcium have been found to inhibit the action of bone-resorbing cells 36 and promote the action of bone-building cells.37

Healthy brain function depends on a normal supply of amino acids, some of which are converted into important brain chemicals. Whey protein contains tryptophan, which the brain uses to make serotonin, a neurotransmitter involved in regulating mood and coping with stress. One group of volunteers was given a whey protein supplement or a placebo in a double-blind trial. The whey protein increased blood tryptophan levels and helped these people maintain a healthy mood while under stress.38

Ingredient Highlights:

Whey is a complete animal source protein comprising all eight essential amino acids. It has been given the highest possible Protein Digestibility Corrected Amino Acid Score (PDCAAS) (1.0). This score is an indication of the quality of a protein and is the foundation for the determination of the FDA’s Daily Reference Value of protein (50 grams). Egg and milk proteins, as well as soy isolate, rank the highest in protein content, surpassing all other sources.

Healthy Whey™ is a great tasting, sugar-free, protein with a natural vanilla flavor. Green-Whey Pro-96™ starts with that same great tasting, sugar-free, protein and adds a food base of Hawaiian Spirulina algae ("Kona pure"), psyllium seed husk, apple pectin, oat fiber, lemon bioflavonoids, kelp, barley grass and the digestive enzymes bromelain (from pineapple) and papain (from papaya).

These additional ingredients provide a nutritious and all-natural combination of protein, fiber, minerals, and phytonutrients including carotenoids. These phytonutrients are the source of natural food colors (pigments) and have been studied extensively for their value. The more intense the color, the more beneficial the food. Maintaining high levels of carotenoids in body tissue helps to encourage healthy cell membranes. While carotenoids are fat-soluble, flavonoids are water-soluble, and have similar antioxidant properties.39,40,41

Safety & Contraindications: Whey has a long historical record as a safe food for lactose-tolerant people. While the possibility of food allergies from whey has to be considered, it has been found to be far less allergenic than the milk protein casein, and possibly less allergenic than soy or egg-based protein supplements.42 All whey proteins contain some lactose. Nature’s Life uses production methods that yield whey with 5% lactose.

The bovine serum albumin (BSA) component of whey has been implicated as a possible trigger for insulin-dependent diabetes mellitus (IDDM) in children. A similarity exists between the amino acid sequence of the beta cell protein found in the pancreas, and BSA. It has been proposed that partially digested fragments of BSA stimulate the immune system that then incorrectly destroys beta cells.43 Currently, the exact nature of the relationship between BSA and IDDM remains unclear. Until more is known, whey supplementation in infants and young children should probably be avoided. As with all food concentrates, consultation with health practitioners is recommended.

References:

  1. Kelly G. Sports nutrition for endurance athletes. Alt Med Rev 1997;2(3):186-201.

  2. Roos N, Mahe S, Benamouzig R, et al. 15N-labeled immunoglobulins from bovine colostrum are partially resistant to digestion in human intestine. J Nutr 1995;125:1238-44.

  3. Mahe S, Roos N, Benamouzig R, et al. Gastrojejunal kinetics and the digestion of (15N) beta-lactoglobulin and casein in humans: the influence of the nature and quality of the protein. Am J Clin Nutr 1996;63:546-552.

  4. Lemon PW. Do athletes need more dietary protein and amino acids? Int J Sport Nutr 1995;5(Suppl):S39-S61.

  5. Tarnopolsky MA, Atkinson SA, MacDougall JD, et al. Evaluation of protein requirements for trained strength athletes. J Appl Physiol 1992;73:1986-95.

  6. Lands LC, Grey VL, Smountas AA. Effect of supplementation with a cysteine donor on muscular performance. J Appl Physiol 1999;87:1381-5.

  7. Demling RH, DeSanti L. Effect of a hypocaloric diet, increased protein intake and resistance training on lean mass gains and fat mass loss in overweight police officers. Ann Nutr Metab 2000;44:21-9.

  8. Melichar V, Mikova M. Feminar with whey (serum) proteins prepared by thermal denatuation. Nitrogen and lipid balance in neonates with a low birth weight. Cesk Pediatr 1989;44:1-5.

  9. Mahan DC. Efficacy of dried whey and its lactalbumin and lactose components at two dietary lysine levels on post weaning pig performance and nitrogen balance. J Anim Sci 1992;70:2182-2187.

  10. Alexander JW, Gottschlich MM. Nutritional modulation in burn patients. Crit Care Med 1990;18:S149-S153.

  11. Bounous G, Baruchel S, Falutz J, et al. Whey proteins as a food supplement in HIV-seropositive individuals. Clin Invest Med 1993;16:204-209.

  12. Blomstrand E, Ek S, Newsholme EA. Influence of ingesting a solution of branched-chain amino acids on plasma and muscle concentrations of amino acids during prolonged submaximal exercise. Nutrition 1996;12:485-490.

  13. MacLean, DA, Graham TE, Satlin B. Branched-chain amino acids augment ammonia metabolism while attenuating protein breakdown during exercise. Am J Physiol 1994;267:E1010-22.

  14. Kanter MM. Free radicals, exercise, and antioxidant supplementation. Proc Nutr Soc 1998;57:9-13.

  15. Leeuwenburgh C, Leichtweis S, Hollander J, et al. Effect of acute exercise on glutathione deficient heart. Mol Cell Biochem 1996;156:17-24.

  16. Shepard RJ, Shek PN. Heavy exercise, nutrition and immune function: is there a connection? Int J Sports Med 1995;16:491-497.

  17. Micke P, Beeh KM, Schlaak JF, Buhl R. Oral supplementation with whey proteins increases plasma glutathione levels of HIV-infected patients. Eur J Clin Invest 2001 Feb;31:171-8.

  18. Ford J, Wong C, Colditz I. Effects of dietary protein types on immune responses and levels of infection with Eimeria vermiformis in mice. Immunol Cell Biol 2001;79:23-8.

  19. Minehira K, Inoue S, Nonaka M, et al. Effects of dietary protein type on oxidized cholesterol-induced alteration in age-related modulation of lipid metabolism and indices of immune function in rats. Biochim Biophys Acta 2000;1483:141-53.

  20. Wong KF, Middleton N, Montgomery M, et al. Immunostimulation of murine spleen cells by materials associated with bovine milk protein fractions. J Dairy Sci 1998;81:1825-32.

  21. Hakansson A, Svensson M, Mossberg AK, et al. A folding variant of alpha-lactalbumin with bactericidal activity against Streptococcus pneumoniae. Mol Microbiol 2000;35:589-600.

  22. Pihlanto-Leppala A, Marnila P, Hubert L, et al. The effect of alpha-lactalbumin and beta-lactoglobulin hydrolysates on the metabolic activity of Escherichia coli JM103. J Appl Microbiol 1999;87:540-5.

  23. Svensson M, Hakansson A, Mossberg AK, et al. Conversion of alpha-lactalbumin to a protein inducing apoptosis. Proc Natl Acad Sci U S A 2000;97:4221-6.

  24. Hakansson A, Andreasson J, Zhivotovsky B, Multimeric alpha-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei. Exp Cell Res 1999;246:451-60.

  25. Hakansson A, Zhivotovsky B, Orrenius S, et al. Apoptosis induced by a human milk protein. Proc Natl Acad Sci U S A 1995;92:8064-8.

  26. Tsuda H, Sekine K, Ushida Y, et al. Milk and dairy products in cancer prevention: focus on bovine lactoferrin. Mutat Res 2000 Apr;462:227-33.

  27. Bounous G. Whey protein concentrate (WPC) and glutathione modulation in cancer treatment. Anticancer Res 2000;20:4785-92.

  28. Kennedy RS, Konok GP, Bounous G, et al. The use of a whey protein concentrate in the treatment of patients with metastatic carcinoma: a phase I-II clinical study. Anticancer Res. 1995;15:2643-9.

  29. Hakkak R, Korourian S, Shelnutt SR, et al. Diets containing whey proteins or soy protein isolate protect against 7,12-dimethylbenz(a)anthracene-induced mammary tumors in female rats. Cancer Epidemiol Biomarkers Prev 2000;9:113-7.

  30. Yamamoto N, Maeno M, Takano T. Purification and characterization of an antihypertensive peptide from a yogurt-like product fermented by Lactobacillus helveticus CPN4. J Dairy Sci 1999;82:1388-93.

  31. Abubakar A, Saito T, Kitazawa. Structural analysis of new antihypertensive peptides derived from cheese whey protein by proteinase K digestion. J Dairy Sci 1998;81:3131-8.

  32. FitzGerald RJ, Meisel H. Lactokinins: whey protein-derived ACE inhibitory peptides. Nahrung 1999;43:165-7.

  33. Pihlanto-Leppala A, Koskinen P, Piilola K, et al. Angiotensin I-converting enzyme inhibitory properties of whey protein digests: concentration and characterization of active peptides. J Dairy Res 2000;67:53-64.

  34. Minehira K, Inoue S, Nonaka M, et al. Effects of dietary protein type on oxidized cholesterol-induced alteration in age-related modulation of lipid metabolism and indices of immune function in rats. Biochim Biophys Acta 2000 Jan 3;1483(1):141-53.

  35. Kawase M, Hashimoto H, Hosoda M, et al. Effect of administration of fermented milk containing whey protein concentrate to rats and healthy men on serum lipids and blood pressure. J Dairy Sci 2000;83:255-63.

  36. Toba Y, Takada Y, Yamamura J, et al. Milk basic protein: a novel protective function of milk against osteoporosis. Bone 2000;27:403-8.

  37. Yamamura J, Takada Y, Goto M, et al. High mobility group-like protein in bovine milk stimulates the proliferation of osteoblastic MC3T3-E1 cells. Biochem Biophys Res Commun 1999 Jul 22;261:113-7.

  38. Markus CR, Olivier B, Panhuysen GE, et al. The bovine protein alpha-lactalbumin increases the plasma ratio of tryptophan to the other large neutral amino acids, and in vulnerable subjects raises brain serotonin activity, reduces cortisol concentration, and improves mood under stress. Am J Clin Nutr 2000;71:1536-44.

  39. Rice-Evans CA, et al. The relative antioxidant activities of plant-derived polyphenolic flavonoids. Free Radic Res. 1995;22:375-83.

  40. Rice-Evans CA and Miller NJ. Antioxidant activities of flavonoids as bioactive components of food. Biochem Soc Trans 1996;24:790-795.

  41. Havsteen B. Flavonoids, a class of natural products of high pharmacological potency. Biochem Pharmacol. 1983;32:1141-8.

  42. Stoger P, Wuthrich B. Type I allergy to cow milk proteins in adults. A retrospective study of 34 adult milk- and cheese-allergic patients. Int Arch Allergy Immunol 1993;102:399-407.

  43. Karjalainen J, Martin JM, Knip M, et al. A bovine albumin peptide as a possible trigger of insulin-dependent diabetes mellitus. N Engl J Med 1992;327:302-307.17.

 

 

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