Turmeric Bone Broth Protein Powders Lean Factor 1 lb
Turmeric Bone Broth Protein Powders Lean Factor
Turmeric Bone Broth Protein Powders Lean Factor
Turmeric Bone Broth Protein Powders Lean Factor
  • Turmeric Bone Broth Protein Powders Lean Factor 1 lb
  • Turmeric Bone Broth Protein Powders Lean Factor
  • Turmeric Bone Broth Protein Powders Lean Factor
  • Turmeric Bone Broth Protein Powders Lean Factor

Subscribe & Save + Get Free shipping on all Auto-ship Orders

Turmeric Bone Broth



If you are looking for the world’s most nutrient-dense food, our Turmeric Bone Broth deserves your attention.

A wonderful combination of powerful antioxidant-rich superfoods, Turmeric Bone Broth Powder, is in a league of its own.

In fact, we challenge you to find another superfood that has as many positive benefits that are provided by turmeric, bone broth, coconut milk, ginger, and cinnamon. And it still tastes nearly like a dessert.

Our Turmeric Bone Broth powder is an easy to drink broth, has a smooth and creamy texture (but not too thick like milk), is lightly sweet because of the turmeric, ginger, and cinnamon taste, and can be enjoyed cold or hot - just like a soup. And because it’s a powder in a self-locking foil pouch, it is effortless to mix, drink, store, and very convenient for travel.

Each serving of Turmeric Bone Broth contains a careful blend of these superfood Ingredients: 

Bone Broth Powder - A high-quality, nutritious superfood that is sourced and made in the United States. Our Bovine Broth is an excellent way to add significant nutritional value to your diet, highly soluble, non-allergenic, 100% natural, and contains no MSG.

Organic Turmeric Root Powder - Turmeric (non-GMO) is one of nature's most powerful healers. Acting as a strong antioxidant and is well known for its ability to support a healthy inflammation response, turmeric supports a healthy digestive system, brain function, cardiovascular system, and joint health. Turmeric has been used for over 2500 years in India.

Organic Coconut Milk Powder - A Delicious Superfood and high in nutrition, naturally packed with phytonutrients, healthy fats, amino acids, vitamins, and minerals. It contains a rare source of Healthy fats called Medium Chain Triglycerides (MCT’s) that are metabolized more efficiently (faster) in the body than normal fats.

Curcumin Extract Powder - With more than 1000 published studies and over 7000 published articles, curcumin extract is one of the most well researched medicinal plant extracts to date and one of nature's most powerful healers. Turmeric has been used for over 2500 years. When taken with some form of fat (coconut milk powder) and pepper (Piperine extract), it will increase the bioavailability by 100 fold.

Organic Ginger Root Powder - Ginger Root has been mentioned in ancient Chinese, Indian, and Middle Eastern writings, where it has long been prized for its aromatic, culinary, and medicinal properties. Native to southeastern Asia, a region whose cuisines still feature this wonderfully spicy herb, ginger has been renowned for millennia in many areas throughout the world. Ginger has a long tradition of being effective in possibly supporting healthy digestion. Modern scientific research has revealed that ginger possesses numerous therapeutic properties, including antioxidant effects, and may support a healthy inflammation response.

Organic Cinnamon Powder (Cassia) - More than just a simple spice, cinnamon packs a powerful punch in the antioxidant arena. Used for thousands of years to treat various ailments, this amazing spice has abundant research to back it up. Cinnamon is obtained from the inner bark of the cinnamon tree. The bark rolls up while drying in the sun and forms what we know as a cinnamon stick, which is left as is or ground into a fine powder.

Organic Stevia Extract (Debittered) - Stevia is a natural herb native to South America. For centuries, the Guarani Indians had known about the unique advantages of kaa he-he, a native term that translates as “sweet herb.” These native people knew the leaves of the wild stevia shrub had a sweetening power unlike anything else; they commonly used the leaves to enhance bitter medicinal potions' taste. Our Stevia Extract Powder has been enzyme-treated (debittered) to remove the bitter steviosides and improve the overall taste. This is a 100% natural herbal extract with nothing added.

Piperine Extract Powder - Piperine has the ability to support the assimilation of food and herbs that are traditionally harder for the body to metabolize. It may support the inhibition of various enzymes responsible for breaking down nutrients. Piperine has been shown to support brain health because of its ability to cross the blood-brain barrier and support other nutrients to do the same. It may support healthy beta-endorphin and serotonin levels, positively affecting one’s mood. Whether you use it as a supplement or as a part of your daily food intake, piperine from black pepper is a great choice not just to spice up your food but get the most nourishment out of it too.

Suggested Use: Add 1 level tbsp (6g) to 4-6 oz water or add 5 level tbsp (30g) to your favorite smoothie or shake.

Mixing suggestions: To increase flavor and nutritional profile, combine with Extra Rich, Raw, Organic Cacao Powder, Organic Coconut Milk Powder, Gelatinized Maca Root Powder, and Hydrolyzed Collagen Powder.

Ingredients: Bone Broth (Bovine), Organic Turmeric Root, Organic Coconut Milk, Curcumin Extract, Organic Ginger Root, Organic Cinnamon (Cassia), Organic Stevia Extract (Debittered), Piperine Extract.

Other Names: Beef stock, bone stock.

Origin: Raised and processed in USA. Packaged with care in Florida, USA.

How to Maintain Optimum Freshness

This product is 100% natural and minimally processed:
Taste, smell, texture, and color may vary from batch to batch. Go here to learn why our products may naturally vary.

The Important Protections we take to Bring you Safe & Nutritious Superfoods:
Please go here to discover the important steps we take to deliver fresh, quality nutrition.

Bulk Quantities?
Need to order a large quantity of our products? We’d be happy to help! Please contact our Bulk department to discuss the details.

Sources & References

1.Anesey, J., Scott, P., Veis, A., and Chyatte, D.: The Isolation of a Soluble Type III Collagen Precursor from Rat Skin, Biochem Biophys Res Commun 62, 946, 1975

2.Bailey, A., Sims, T., and Light, N.: Cross-Linking in Type IV Collagen, Biochem J 218, 713, 1984

3.Bailey, A., Sims, T., LeLouis, M., and Brazin, S.: Collagen Polymorphism in Experimental Granulation Tissue, Biochem Biophys Res Commun 66, 1160, 1975

4.Bashey, R., Halpem, S., Stephens, R., Perlish, J., and Fleischmajer, R.: Solubility of Collagen from Normal and Scleroderma Fibroblasts in Culture, Biochem Biophys Res Commun 62, 303, 1975

5.Becker, H., Furthmayr, H., and Trimple, R.: Tryptic Peptides from the Cross-Linking Regions of Insoluble Calf Skin Collagen, Physiol Chem 356, 21, 1975

6.Berthet-Colominas, C., Miller, A., Herbage, D., Ronziere, M., and Tocchetti, D.: Structural Studies of Collagen Fibres from Intervertebral Disc, Biochim Biophys Acta 706, 50, 1982

7.Birk, D., Fitch, J., Babiarz, J., Doane, K., and Linsenmayer, T.: Collagen Fibrilogenesis in vitro: Interaction of Types I and V Collagen Regulates Fibril Diameter, J Cell Sci 95, 649, 1990

8.Bornstein, P., and Sage, H.: Structurally Distinct Collagen Types, Annu Rev Biochem 49, 957, 1980

9.Bruckner, P., and van der Rest, M.: Structure and Function of Cartilage Collagens, Microsc Res Tech 28, 378, 1994

10.Bruns, R.: Beaded Filaments and Long-Spacing Fibrils: Relation to Type VI Collagen, J Ultrastruct Res 89, 136, 1984

11.Burgeson, R., and Nimni, M.: Collagen Types - Molecular Structure and Tissue Distribution, Clin Orthop 282, 250, 1992

12.Butler, W., Henning, B., Beegle, W., Taylor, R., and Chung, E.: Proteins of the Periodontium. Identification of Collagens with the [alpha-1(I)]2 alpha-2 and [alpha-1(III)]3 Structures in Bovine Periodontal Ligament, J Biol Chem 250, 8907, 1975

13.Campa, J., McAnulty, R., and Laurent, G.: Application of High-Pressure Liquid Chromatography to Studies of Collagen Production by Isolated Cells in Culture, Anal Biochem 186, 257, 1990

14.Canalis, E., McCarthy, T., and Centrella, M.: Differential Effects of Continuous and Transient Treatment with Parathyroid Hormone Related Peptide (PHrp) on Bone Collagen Synthesis, Endocrinology 126, 1806, 1990

15.Cannon, J., and Cintron, C.: Collagen Cross-Linking in Corneal Scar Formation, Biochim Biophys Acta 412, 18, 1975

16.Charonis, A., and Tsilibary, E.: Structural and Functional Changes of Laminin and Type-IV Collagen after Nonenzymatic Glycation, Diabetes 41, 49, 1992

17.Chesney, C., Harper, E., and Colman, R.: Critical Role of the Carbohydrate Side Chains of Collagen in Platelet Aggregation, J Clin Invest 51, 2693, 1972

18.Cheung, D., DiCesare, P., Benya, P., Libow, E., and Nimni, M.: The Presence of Intermolecular Disulfide Crosslinks in Type III Collagen, J Biol Chem 258, 7774, 1983

19.Chiang, T., Beachey, E., and Kang, A.: Interaction of a Chick Skin Collagen Fragment (alpha1-CB5) with Human Platelets. Biochemical Studies During the Aggregation and Release Reaction, J Biol Chem 250, 6916, 1975

20.Cooper, D., and Davidson, R.: The Effect of Ultraviolet Irradiation on Collagen-Fold Formation, Biochem J 98, 655, 1966

21.Cooper, D., and Davidson, R.: The Effect of Ultraviolet Irradiation on Soluble Collagen, Biochem J 97, 139, 1965

22.Daniels, J., and the Chu, G.: Basement Membrane Collagen of Renal Glomerulus, J Biol Chem 250, 3531, 1975

23.Davidson, J., McEneany, L., and Bornstein, P.: Intermediates in the Limited Proteolytic Conversion of Procollagen to Collagen, Biochemistry 14, 5188, 1975

24.Davis, N.: Stable Crosslinks of Collagen, Biochem Biophys Res Commun 54, 914, 1973

25.Davis, N., Risen, O., and Pringle, G.: Stable Nonreducible Cross-Links of Mature Collagen, Biochemistry 14, 2031, 1975

26.Davison, P.: Diamines and Aminoalcohols: Neutral Solvents for Native Collagen, Conn Tissue Res 24, 129, 1990

27.Davison, P., and Brennan, M.: Collagenase Digestion Demonstrates Carboxy-Terminal Crosslinking in Acid-Soluble Collagen, Biochim Biophys Acta 708, 141, 1982

28.Deshmukh, K., and Nimni, M.: Effects of Lysosomal Enzymes on the Type of Collagen Synthesized by Bovine Articular Cartilage, Biochem Biophys Res Commun 53, 424, 1973

29.Diegelmann, R., Bryson, G., Flood, L., and Graham, M.: A Microassay to Quantitate Collagen Synthesis by Cells in Culture, Anal Biochem 186, 296, 1990

30.Dixit, S., Kang, A., and Gross, J.: Covalent Structure of Collagen: Amino Acid Sequence of alpha1-CB3 of Chick Skin Collagen, Biochemistry 14, 1929, 1975

31.Dixit, S., Seyer, J., Oronsky, A., Corbett, C., Kang, A., and Gross, J.: Covalent Structure of Collagen: Amino Acid Sequence of alpha1-CB6A of Chick Skin Collagen, Biochemistry 14, 1933, 1975

32.Doyle, B., Hukins, D., Hulmes, D., Miller, A., Rattew, C., and Woodhead-Galloway, J.: Origins and Implication of the D Stagger in Collagen, Biochem Biophys Res Commun 60, 858, 1974

33.Drake, M., Davison, P., Bump, S., and Schmitt, F.: Action of Proteolytic Enzymes on Tropocollagen and Insoluble Collagen, Biochemistry 5, 301, 1966

34.Dublet, B., and van der Rest, M.: Type XII Collagen is Expressed in Embryonic Chick Tendons. Isolation of Pepsin-Derived Fragments, J Biol Chem 262, 17724, 1987

35.Einbinder, J., and Schubert, M.: Binding of Mucopolysaccharides and Dyes by Collagen , J Biol Chem 188, 335, 1951

36.Elliot, R., and Gardner, D.: A Comparison of Acid-Ninhydrin and Isolation Methods for the Measurement of Proline in Collagen Hydrolysates, Biochem Soc Trans 2, 741, 1975

37.Epstein, E., and Munderloh, N.: Isolation and Characterization of CNBr Peptides of Human [alpha-1(III)]3Collagen and Tissue Distribution of [alpha-1(I)]2alpha-2 and [alpha-1(III)]3 Collagens, J Biol Chem 250, 9304, 1975

38.Etherington, D.: The Purification of Bovine Cathepsin B1 and its Mode of Action on Bovine Collagens, Biochem J 137, 547, 1974

39.Evans, C., and Drouven, B.: The Promotion of Collagen Polymerization by Lanthanide and Calcium Ions, Biochem J 213, 751, 1983

40.Eyre, D., Paz, M., and Gallop, P.: Cross-Linking in Collagen and Elastin, Annu Rev Biochem 53, 717, 1984

41.Ferwerda, W., Feltkamp-Vroom, T., and Smit, J.: Collagen and Glycoprotein Components Derived from Bovine Tubular Basement Membrane: Chemical and Immunological Properties, Biochem Soc Trans 2, 640, 1975

42.Fietzek, P., and Kuhn, K.: The Covalent Structure of Collagen: Amino Acid Sequence of the N-Terminal Region of alpha2-CB5 from Rat Skin Collagen, F.E.B.S. Lett. 36, 289, 1973

43.Fietzek, P., and Kuhn, K.: The Covalent Structure of Collagen: Amino-Acid Sequence of the Cyanogen-Bromide Peptides alpha1-CB2, alpha1-CB4 and alpha1-CB5 from Calf-Skin Collagen, Eur J Biochem 52, 77, 1975

44.Fietzek, P., and Rexrodt, F.: The Covalent Structure of Collagen. The Amino-Acid Sequence of alpha 2-CB4 from Calf-Skin Collagen, Eur J Biochem 59, 113, 1975

45.Fietzek, P., Rexrodt, F., Hopper, K., and Kuhn, K.: The Covalent Structure of Collagen. 2. The Amino-Acid Sequence of alpha 1-CB7 from Calf Skin Collagen, Eur J Biochem 38, 396, 1973

46.Fine, A., Poliks, C., Smith, B., and Goldstein, R.: The Accumulation of Type I Collagen mRNAs in Human Embryonic Lung Fibroblast Stimulated by Transforming Growth Factor beta, Conn Tissue Res 24, 237, 1990

47.Folkhard, W., Geercken, W., Knorzer, E., Mosler, E., Nemetschek-Gansler, H., Nemetschek, T., and Koch, M.: Structural Dynamic of Native Tendon Collagen , J Mol Biol 193, 405, 1987

48.Fuji, K., Corcoran, D., and Tanzer, M.: Isolation and Structure of a Cross-Linked Tripeptide from Calf Bone Collagen, Biochemistry 14, 4409, 1975

49.Fujimori, E.: Changes Induced by Ozone and Ultraviolet Light in Type I Collagen. Bovine Achilles Tendon Collagen versus Rat Tail Tendon Collagen, Eur J Biochem 152, 299, 1985

50.Fujimori, E., and Shambaugh, N.: Cross-Linking and Fluorescence of Pyrene-Labeled Collagen, Biochim Biophys Acta 742, 155, 1983

51.Fukae, M., Mechanic, G., Adamy, L., and Schwartz, E.: Chromatographically Different Type II Collagens from Human Normal and Osteoarthritic Cartilage, Biochem Biophys Res Commun 67, 1575, 1975

52.Gallop, P., and Seifter, S.: Preparation and Properties of Soluble Collagen, Methods Enzymol 6, 635, 1963

53.Gay, S., and Miller, E.: What is Collagen, What is Not, Ultrastruct Pathol 4, 365, 1983

54.Glowacki, J., and Gross, J.: Self Assembly of Mixtures of Collagen alpha-Chains, Biochim Biophys Acta 668, 216, 1981

55.Gordon, M., Gerecke, D., and Olsen, B.: Type XII Collagen: Distinct Extracellular Matrix Component Discovered by cDNA Cloning, Proc Natl Acad Sci U S A 84, 6040, 1987

56.Gordon, M., Gerecke, D., Dublet, B., van der Rest, M., Sugrue, S., and Olsen, B.: The Structure of Type XII Collagen, Ann N Y Acad Sci 580, 8, 1990

57.Grillo, H., and Gross, J.: Thermal Reconstitution of Collagen from Solution and the Response to its Heterologous Implantation, J Surg Res 2, 69, 1962

58.Haidar, A., Wigglesworth, J., and Krausz, T.: Type IV Collagen in Developing Human Lung: A Comparison Between Normal and Hypoplastic Fetal Lungs, Early Human Devt 21, 175, 1990

59.Hamlin, C., Kohn, R., and Luschin, J.: Apparent Accelerated Aging of Human Collagen in Diabetes Mellitus, Diabetes 24, 902, 1975

60.Hanada, E., and Anan, F.: Isolation and Properties of the Insoluble Collagen Fraction from Bovine Nasal Septal Cartilage, J. Biochem. 74, 505, 1973

61.Hayashi, T., and Nagai, Y.: Effect of pH on the Stability of Collagen Molecule in Solution, J. Biochem. 73, 999, 1973

62.Hayashi, T., and Nagai, Y.: Time-Dependent Increase in Stability of Collagen Fibrils Formed in vitro. Effect of Temperature, J. Biochem. 75, 651, 1974

63.Helseth, D., and Veis, A.: Collagen Self-Assembly in vitro. Differentiating Specific Telopeptide-Dependent Interactions Using Selective Enzyme Modification and the Addition of Free Amino Telopeptide, J Biol Chem 256, 7118, 1981

64.Hessle, H., and Engvall, E.: Type VI Collagen. Studies on its Localization, Structure, and Biosynthetic Form with Monoclonal Antibodies, J Biol Chem 259, 3955, 1984

65.Highberger, J., Corbett, C., Kang, A., and Cross, J.: The Amino Acid Sequence of Chick Skin Collagen alpha 1-CB7, Biochemistry 14, 2872, 1975

66.Hirai, K., Shimizu, Y., and Hino, T.: Epithelial Regeneration in Collagen-Coated and Uncoated Patch Grafts Implanted into Dog Tracheas, J Exp Pathol 71, 51, 1990

67.Housley, T., Tanzer, M., Henson, E., and Gallop, P.: Collagen Crosslinking: Isolation of Hydroxyaldol-Histidine, a Naturally-Occurring Crosslink, Biochem Biophys Res Commun 67, 824, 1975

68.Hudson, B., Wieslander, J., Wisdom, B., and Noelken, M.: Goodpasture Syndrome: Molecular Architecture and Function of Basement Membrane Antigen, Lab Invest 61, 256, 1989

69.Hunt, E., and Morris, H.: Collagen Cross-Links. A Mass-Spectrometric and G- and 13C-Nuclear Magnetic-Resonance Study, Biochem J 135, 833, 1973

70.Igarashi, S., Trelstad, R., and Kang, A.: Physical and Chemical Properties of Chick Cartilage Collagen, Biochim Biophys Acta 295, 514, 1973

71.Jamieson, G., Urban, C., and Barber, A.: Enzymatic Basis for Platelet Aggregation: Collagen Adhesion as the Primary Step in Haemostasis, Nature New Biol 234, 5, 1971

72.Jander, R., Troyer, D., and Rauterberg, J.: A Collagen-Like Glycoprotein of the Extracellular Matrix is the Undegraded Form of Type VI Collagen, Biochemistry 23, 3675, 1984

73.Kahn, L., and Wittnauer, L.: The Viscometric Behavior of Solubilized Calf Skin Collagen at Low Rates of Shear, J Biol Chem 241, 1784, 1966

74.Kapoor, R., Sakai, L., Funk, S., Roux, E., Bornstein, P., and Sage, E.: Type VIII Collagen Has a Restricted Distribution in Specialized Extracellular Matrices, J Cell Biol 107, 721, 1988

75.Kasten, M., Burkhardt, H., von Roden, H., and Rauls, S.: A Spectroscopic Collagenase Assay Using Peroxidase-Labeled Collagen, Anal Biochem 176, 150, 1989

76.Katzman, R., Kang, A., and Beachey, E.: Collagen-Induced Platelet Aggregation: Involvement of an Active Glycopeptide Fragment (a1-CB5), Science 181, 670, 1973

77.Keene, D., Engvall, E., and Glanville, R.: Ultrastructure of Type VI Collagen in Human Skin and Cartilage Suggests an Anchoring Function for This Filamentous Network, J Cell Biol 107, 1995, 1988

78.Kittelberger, R., Davis, P., Flynn, D., and Greenhill, N.: Distribution of Type VIII Collagen in Tissues: An Immunohistochemical Study, Conn Tissue Res 24, 303, 1990

79.Lampiaho, K., Kari, A., Niinikoski, J., and Kulonen, E.: Time Course of Action of Pepsin on Insoluble and Soluble Collagens, Acta Chem Scand 20, 1446, 1966

80.Lenaers, A., and Lapiere, C.: Type III Procollagen and Collagen in Skin , Biochim Biophys Acta 400, 121, 1975

81.Lichenstein, J., Byers, P., Smith, B., Martin, G.: Identification of the Collagenous Proteins Synthesized by Cultured Cells from Human Skin, Biochemistry 14, 1589, 1975

82.Lunstrum, G., Mcdonough, A., Marinkovich, M., Keene, D., Morris, N., and Burgeson, R.: Identification and Partial Purification of a Large, Variant Form of Type-XII Collagen, J Biol Chem 267, 20087, 1992

83.Meredith, S., and Kezdy, F.: The Chromatographic Purification of Native Types I, II and III Collagens, Biochim Biophys Acta 668, 357, 1981

84.Miller, E., and Matukas, V.: Chick Cartilage Collagen: A New Type of alpha 1 Chain Not Present in Bone or Skin of the Species, Proc Natl Acad Sci U S A 64, 1264, 1969

85.Mitchell, T., and Rigby, B.: in vivo and in vitro Aging of Collagen Examined Using an Isometric Melting Technique, Biochim Biophys Acta 393, 531, 1975

86.Mustard, J., Cazenave, J., Packham, M., and Toronto, H.: Adherence of Platelets to a Collagen-Coated Surface: Development of a Quantitive Method, J Lab Clin Med 82, 978, 1973

87.Myers, J., Jones, T., Pohjolainen, E., Kadri, A., Goddard, A., Sheer, D., Solomon, E., and Pihlajaniemi, T.: Molecular Cloning of alpha 5(IV) Collagen and Assignment of the Gene to the Region of the X Chromosome Containing the Alport Syndrome Locus, Am J Hum Genet 46, 1024, 1990

88.Na, G.: Interaction of Calf Skin Collagen with Glycerol: Linked Function Analysis, Biochemistry 25, 967, 1986

89.Na, G., Butz, L., and Carroll, R.: Mechanism of in vitro Collagen Assembly. Kinetic and Morphological Studies, J Biol Chem 261, 12290, 1986

90.Nakanishi, M., Imamura, H., and Goto, K.: Potentiation of the ADP-Induced Platelet Aggregation by Collagen and its Inhibition by a Tetrahydrothieno-Pyridine Derivative (gamma-3642), Biochem Pharmacol 20, 2116, 1971

91.Negro, A., Garbisa, S., Gotte, L., and Spina, M.: The Use of Reverse-Phase High-Performance Liquid Chromatography and Precolumn Derivatization with Dansyl Chloride for Quantitation of Specific Amino Acids in Collagen and Elastin, Anal Biochem 160, 39, 1987

92.Newman, R., and Langner, R.: Comparison of TCA and Collagenase in the Isolation of Tissue Collagen, Anal Biochem 66, 175, 1975

93.Obrink, B., Laurent, T., and Carlsson, B.: The Binding of Chondroitin Sulphate to Collagen, F.E.B.S. Lett. 56, 166, 1975

94.Oikawa, T., Sayama, K., Matsuda, Y., Fujimoto, Y., Iwaguchi, T., and Matsuzawa, A.: Characterization of Two Possible Forms of Type IV Collagen from Human Kidney Cortex, Biochem Int 19, 615, 1989

95.Ono, M., Aratani, Y., Kitagawa, I., and Kitagawa, Y.: Ascorbic Acid Phosphate Stimulates Type IV Collagen Synthesis and Accelerates Adipose Conversion of 3T3-L1 Cells, Exp Cell Res 187, 309, 1990

96.Ooshima, A., Fuller, G., Cardinale, G., Spector, S., and Udenfriend, S: Collagen Biosynthesis in Blood Vessels of Brain and Other Tissues of the Hypertensive Rat, Science 190, 898, 1975

97.Oryan, A., Moshiri, A., Meimandi-Parizi, A., and Maffulli, N.: Role of Xenogenous Bovine Platelet Gel Embedded within Collagen Implant on Tendon Healing: An in vitro and in vivo Study. , Exp Biol Med 240, 194, 2015

98.Packman, M., and Guccione, M.: Inhibition of the Platelet Responses to Synergistic Effects of Collagen and ADP, Fed Proc 32, 844, 1973

99.Pardo, A., and Tamayo, R.: The Presence of Collagenase in Collagen Preparations, Biochim Biophys Acta 392, 121, 1975

100.Parreno, J., Raju, S., Niaki, M., Andrejevic, K., Jiang, A., Delve, E., and Kandel, R.: Expression of Type I Collagen and Tenascin C is Regulated by Actin Polymerization Through MRTF in Dedifferentiated Chondrocytes, F.E.B.S. Lett. 588, 3677, 2014

101.Piez, K., and Torchida, D.: Possible Contribution of Ionic Clustering to Molecular Packing of Collagen, Nature 258, 87, 1975

102.Puett, D., and Cunningham, L.: Effect of Collagen Modification on Platelet Aggregation, Fed Proc 32, 614, 1973

103.Puett, D., Wasserman, B., Ford, J., and Cunningham, L.: Collagen-mediated Platelet Aggregation. Effects of Collagen Modification Involving the Protein and Carbohydrate Moieties, J Clin Invest 52, 2495, 1973

104.Quteish, D., Singh, G., and Dobly, A.: Development and Testing of a Human Collagen Graft Material, J Biomed Mater Res 24, 749, 1990

105.Rexrodt, F., Fietzek, P., and Kuhn, K.: The Covalent Structure of Collagen. The Chymotrypsin, Trypsin and Hydroxylamine Peptides Derived form alpha2-CB4 of Calf-Skin Collagen, Eur J Biochem 59, 105, 1975

106.Rexrodt, F., Hopper, K., Fietzek, P., and Kuhn, K.: The Covalent Structure of Collagen. 1. The Chymotrypsin, Trypsin and Thermolysin-Derived Peptides of alpha1-CB7 from Calf-Skin Collagen, Eur J Biochem 38, 384, 1973

107.Ricard-Blum, S.: The Collagen Family, Cold Spring Harb Perspect Biol 3, a004978, 2011

108.Robertson, W., Rose, K., Hudson, B., and Vanacore, R.: Supramolecular Organization of the alpha121-alpha565 Collagen IV Network, J Biol Chem 289, 25601, 2014

109.Robins, S., and Bailey, A.: The Chemistry of the Collagen Cross-Links. The Characterization of Fraction C, a Possible Artifact Produced During the Reduction of Collagen Fibres with Borohydride, Biochem J 135, 657, 1973

110.Robins, S., and Bailey, A.: The Chemistry of the Collagen Cross-Links. The Mechanism of Stabilization of the Reducible Intermediate Cross-Links, Biochem J 149, 381, 1975

111.Robins, S., Shimokomaki, M., and Bailey, A.: The Chemistry of the Collagen Cross-Links. Age-Related Changes in Reducible Components of Intact Bovine Collagen Fibres, Biochem J 131, 771, 1973

112.Roelofs, L., Kortmann, B., Oosterwijk, E., Eggink, A., Tiemessen, D., Crevels, A., Wijnen, R., Daamen, W., van Kuppevelt, T., Geutjes, P., and Feitz, W.: Tissue Engineering of Diseased Bladder Using a Collagen Scaffold in a Bladder Exstrophy Model, BJU Int 114, 447, 2014

113.Russell, A.: Effect of pH on Thermal Stability of Collagen in the Dispersed and Aggregated States, Biochem J 139, 277, 1974

114.Ryhanen, L., Zaragoza, E., and Uitto, J.: Conformational Stability of Type 1 Collagen Triple Helix: Evidence for Temporary and Local Relaxation of the Protein Conformation Using a Proteolytic Probe, Arch Biochem Biophys 223, 562, 1983

115.Salem, G., and Traub, W.: Conformation Implications of Amino Acid Sequence Regularities in Collagen, F.E.B.S. Lett. 51, 94, 1975

116.Sandberg, M., Tamminen, M., Hirvonen, H., Vuorio, E., and Pihlajaniemi, T.: Expression of mRNAs Coding for the alpha 1 Chain of Type XIII Collagen in Human Fetal Tissues: Comparison with Expression of mRNAs for collagen types I, II, and III, J Cell Biol 109, 1371, 1989

117.Schmid, T., and Linsenmayer, T.: Denaturation-Renaturation Properties of Two Molecular Forms of Short-Chain Cartilage Collagen, Biochemistry 23, 553, 1984

118.Scott, P.: Spectroscopic Study of Environment-Dependent Changes in the Conformation of the Isolated Carboxy-Terminal Telopeptide of Type I Collagen, Biochemistry 25, 974, 1986

119.Seifter, S., and Gallop, P.: The Proteins, 2nd ed Vol. IV, H. Neurath, Academic Press, NY, 238, 1966

120.Shen, G., Butkowski, R., Cheng, T., Wieslander, J., Katz, A., Cass, J., and Fish, R.: Comparison of Non-collagenous Type IV Collagen Subunits in Human Glomerular Basement Membrane, Alveolar Basement Membrane, and Placenta, Conn Tissue Res 24, 289, 1990

121.Shuttleworth, C., and Forrest, L.: Changes in Guinea-Pig Dermal Collagen During Development, Eur J Biochem 55, 391, 1975

122.Shuttleworth, C., Forrest, L., and Jackson, D.: Comparison of the Cyanogen Bromide Peptides of Insoluble Guinea-Pig Skin and Scar Collagen, Biochim Biophys Acta 379, 207, 1975

123.Siegel, R., and Lian, J.: Lysyl Oxidase Dependent Synthesis of a Collagen Cross-Link Containing Histidine, Biochem Biophys Res Commun 67, 1353, 1975

124.Stanley, N., Alper, R., Cunningham, E., Cherniack, N., and Kefalides, N.: Effects of a Molecular Changes in Collagen on Lung Structure and Mechanical Function, J Clin Invest 55, 1195, 1975

125.Stevens, F., and Thomas, H.: Preparation of Insoluble Collagen from Human Cartilage, Biochem J 135, 245, 1973

126.Stinson, R.: Structural Deterioration of Tendon Collagen in Genetic Muscular Dystrophy, Biochim Biophys Acta 400, 255, 1975

127.Sugrue, S., Gordon, M., Seyer, J., Dublet, B., van der Rest, M., and Olsen, B.: Immunoidentification of Type XII Collagen in Embryonic Tissues, J Cell Biol 109, 939, 1989

128.Swann, D., Chesney, C., Constable, I., Colman, R., Caulfield, J., and Harper, E.: The Role of Vitreous Collagen in Platelet Aggregation in vitro and in vivo, J Lab Clin Med 84, 264, 1974

129.Tanzer, M., Housley, T., Berube, L., Fairweather, R., Franzblau, C., and Gallop, P.: Structure of Two Histidine-Containing Cross-Links from Collagen, J Biol Chem 248, 393, 1973

130.Tekari, A., Luginbuehl, R., Hofstetter, W., and Egli, R.: Chondrocytes Expressing Intracellular Collagen Type II Enter the Cell Cycle and Co-Express Collagen Type I in Monolayer Culture, J Orthop Res 32, 1503, 2014

131.Terajima, M., Perdivara, I., Sricholpech, M., Deguchi, Y., Pleshko, N., Tomer, K., and Yamauchi, M.: Glycosylation and Cross-Linking in Bone Type I Collagen, J Biol Chem 289, 22636, 2014

132.Thomas, J., Ayad, S., and Grant, M.: Cartilage Collagens: Strategies for the Study of Their Organisation and Expression in the Extracellular Matrix, Ann Rheum Dis 53, 488, 1994

133.Toole, B., and Lowther, D.: Precipitation of Collagen Fibrils in vitro by Protein Polysaccharides, Biochem Biophys Res Commun 29, 515, 1967

134.Torbet, J., and Ronziere, M.: Magnetic Alignment of Collagen During Self-Assembly, Biochem J 219, 1057, 1984

135.Tristram, G., Worral, J., and Streer, D.: Thermal Denaturation of Soluble Calf Skin Collagen, Biochem J 95, 350, 1965

136.Tseng, S., Savion, N., Gospodarowicz, D., and Stern, R.: Characterization of Collagens Synthesized by Cultured Bovine Corneal Endothelial Cells, J Biol Chem 256, 3361, 1981

137.Uitto, J., Hoffmann, H., and Prockop, K.: Retention of Nonhelical Procollagen Containing cis-Hydroxyproline in Rough Endoplasmic Reticulum, Science 190, 1202, 1975

138.Venkatasubramanian, K., Saini, R., and Vieth, W.: On the Mechanism of Enzyme and Whole Microbial Cell Attachment to Collagen, Ferm Tech 52, 268, 1974

139.Venn, G., Mehta, M., and Mason, R.: Characterization of Collagen from Normal and Scoliolic Human Spinal Ligament, Biochim Biophys Acta 757, 259, 1983

140.Verzar, F., and Stritmattier-Ackershott, E.: Studies on Ageing of Collagen by Perchlorate Reactions, Experientia 31, 1183, 1975

141.Wang, S., and Vieth, W.: Collagen-Enzyme Complex Membranes and Their Performance in Biocatalytic Modules, Biotechnol Bioeng 15, 93, 1973

142.Weber, S., Engel, J., Wiedemann, H., Glanville, R., and Timple, R.: Subunit Structure and Assembly of the Globular Domain of Basement-Membrane Collagen Type IV, Eur J Biochem 139, 401, 1984

143.Weinstock, M., and Leblond, C.: Synthesis, Migration, and Release of Precursor Collagen by Odontoblasts as Visualized by Radioautography After [3H] Proline Administration, J Cell Biol 60, 92, 1974

144.Weiss, J., Shuttleworth, C., Brown, R., and Hunter, J.: Letter: Polymeric Type-III Collagen in Inflamed Human Synovia, Lancet 2, 85, 1975

145.Weiss, J., Shuttleworth, C., Brown, R., Sedowfia, K., Baildam, A., and Hunter, J.: Occurrence of Type III Collagen in Inflamed Synovial Membranes: A Comparison Between Non-Rheumatoid, Rheumatoid, and Normal Synovial Collagens, Biochem Biophys Res Commun 65, 907, 1975

146.Wilkinson, M., Cohen, R., and Shuman M.: A Nonradioactive Assay for Type IV Collagen Degradation, Anal Biochem 185, 294, 1990

147.Woodhead-Galloway, J., Hukins, D., and Wray, J.: Closest Packing of Two-Stranded Coiled-Coils as a Model for the Collagen Fibril, Biochem Biophys Res Commun 64, 1237, 1975

148.Wu, J., and Eyre, D.: Covalent Interactions of Type IX Collagen in Cartilage, Conn Tissue Res 20, 241, 1989

149.Yamaguchi, N., Benya, P., van der Rest, M., and Ninomiya, Y.: The Cloning and Sequencing of alpha 1(VIII) Collagen cDNAs Demonstrate that Type VIII Collagen is a Short Chain Collagen and Contains Triple-Helical and Carboxyl-Terminal Non-Triple-Helical Domains Similar to Those of Type X Collagen, J Biol Chem 264, 16022, 1989

150.Yasui, N., Benya, P., and Nimni, M.: Identification of a Large Interrupted Helical Domain of Disulfide-bonded Cartilage Collagen, J Biol Chem 259, 14175, 1984

151.York, T., Kahan, L., Lake, S., and Gruev, V.: Real-Time High-Resolution Measurement of Collagen Alignment in Dynamically Loaded Soft Tissue, J Biomed Opt 19, 066011, 2014

152.Yurchenco, P., and Furthmayr, H.: Self-Assembly of Basement Membrane Collagen, Biochemistry 23, 1839, 1984

* Reviews & Success Stories Disclaimer

Product reviews solely reflect the views & opinions expressed by the contributors and not those of Lean Factor. Lean Factor does not verify or endorse any claims made in these reviews. Statements have not been evaluated by the FDA and are not intended to diagnose, treat, cure, or prevent any disease or health condition.

Customer Reviews

No reviews yet
Turmeric Bone Broth Protein Powders Lean Factor 1 lb

Turmeric Bone Broth

Customer Reviews

No reviews yet