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Bone Broth Protein Powder



Chicken Bone Broth Protein Concentrate

Integrated process for producing meat protein, broth, myoglobin pigment, fat and bone meal


In accordance with the present invention, there is provided a method for simultaneously producing: natural muscle protein having very low fat and cholesterol content; stabilized myoglobin pigment; broth with superior gelling, emulsifying and film-forming properties; high-quality animal fat; and bone meal with consistent calcium and phosphate content. The above products are produced from comminuted animal carcass by-products which are divided into a solid-phase fraction and a solution-phase fraction. The broth, fat and bone meal products are prepared from the solid-phase fraction, and the protein and pigment products are prepared from the solution-phase fraction.

Lin, Rudy. “Integrated process for producing meat protein, broth, myoglobin pigment, fat and bone meal.” U.S. Patent No. 5,384,149. 24 Jan. 1995.


Protein recovery from mechanically deboned turkey residue by enzymic hydrolysis


Enzymic hydrolysis was used to recover a potentially edible high protein hydrolysate from mechanically deboned turkey residue (MDTR), a turkey processing waste. The hydrolysis process reduced the weight of the original MDTR by 51% on a dry weight basis and recovered 46% of the MDTR proteins. The hydrolysate contained 78% protein, 4·6% ash, and only 5·7% fat. The proteins consisted mainly of amino acids and small peptides with molecular masses lower than 6·5 kD due to a high degree of hydrolysis (65–70%) and were very soluble in water over a wide pH range. It had a yellowish color, was rich in calcium, phosphorus, potassium, and magnesium and had a large monolayer value, but had low viscosity and low emulsion capacity at pH values of 4, 7 and 10. Its buffering capacity was at a minimum between pH 5 and 7.

Fonkwe, L. G., and R. K. Singh. “Protein recovery from mechanically deboned turkey residue by enzymic hydrolysis.” Process Biochemistry 31.6 (1996): 605-616.


Interactions between the bone matrix proteins osteopontin and bone sialoprotein and the osteoclast integrin alpha v beta 3 potentiate bone resorption.


We have investigated the mechanism by which osteoclasts adhere to and resorb bone. We show that these cells express beta 1 and beta 3 integrins which are involved in attachment to purified bone matrix proteins. Binding to osteopontin and bone sialoprotein is mediated by alpha v beta 3, while a beta 1 integrin is responsible for attachment to fibronectin. Both the rapid attachment by osteoclasts to intact bone particles and their subsequent resorption are blocked by a monoclonal antibody directed to the alpha v beta 3 complex but not by an antibody against beta 1 integrins. Attachment of osteoclasts to the bone is also inhibited with soluble osteopontin, Arg-Gly-Asp-containing peptides derived from both osteopontin and bone sialoprotein, or a monospecific polyclonal antibody against osteopontin. We conclude that both osteoclast adherence to the bone and subsequent resorption of its matrix are dependent on interactions between the bone matrix proteins osteopontin and/or bone sialoprotein and the integrin alpha v beta 3. Moreover, collagen, which constitutes 90% of its organic matrix, is minimally involved in binding of chicken osteoclasts to the bone.

Ross, F. Patrick, et al. “Interactions between the bone matrix proteins osteopontin and bone sialoprotein and the osteoclast integrin alpha v beta 3 potentiate bone resorption.” Journal of Biological Chemistry 268.13 (1993): 9901-9907.


Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells.


Two arginine-specific ADP-ribosyltransferase cDNAs (designated AT1 and AT2) were cloned from chicken bone marrow cells. Each cDNA encodes a different peptide of 312 amino acid residues. Homology of deduced amino acid sequences between AT1 and AT2 was 78.3%. We found all six combined peptide sequences of 222 amino acid residues derived from purified chicken heterophil ADP-ribosyltransferase (Mishima, K., Terashima, M., Obara, S., Yamada, K., Imai, K., and Shimoyama, M. (1991) J. Biochem. (Tokyo) 110, 388-394) in the deduced amino acid sequence of AT1, with two amino acid mismatches. Arginine-specific ADP-ribosyltransferase activity was detected in the culture medium of COS 7 cells transiently transfected with AT1 cDNA, while activity from the cells transfected with AT2 cDNA was found in both culture medium and cell lysate. AT1 transferase required 2-mercaptoethanol for the activity. The activity was inhibited in the presence of NaCl while AT2 enzyme was activated by either agent. On zymographic in situ gel analysis, estimated molecular masses of the AT1, AT2, and purified chicken heterophil transferases were 32, 34, and 27.5 kDa, respectively. Northern blot analysis with specific probes to AT1 or AT2 cDNAs revealed about a 1.5-kilobase message in chicken bone marrow cells but no signals were observed in heterophils, spleen, and liver of chicken or human HL-60 cells. Highly conserved regions were observed among the deduced amino acid sequences of AT1, AT2, rabbit skeletal muscle transferase, and rodent T-cell surface antigen RT6s.

Tsuchiya, Mikako, et al. “Cloning and expression of cDNA for arginine-specific ADP-ribosyltransferase from chicken bone marrow cells.” Journal of Biological Chemistry 269.44 (1994): 27451-27457.


Purification and characterization of cMGF, a novel chicken myelomonocytic growth factor.


We describe the purification of a novel hematopoietic growth factor from the conditioned medium of a transformed macrophage cell line. The factor, termed chicken myelomonocytic growth factor (cMGF) stimulates the growth of chicken myeloblasts transformed by myb oncogene‐containing retroviruses and induces the formation of macrophage colonies in uninfected chick bone marrow cultures. The biological activity of the factor is destroyed by trypsin and by reducing reagents but not by SDS. Analysis of crude conditioned medium on non‐reducing SDS gels reveals two active species of cMGF with mol. wts. of 23 and 27 kd. Incubation of radioiodinated partially purified cMGF with myeloblasts demonstrates the specific binding of 23‐ and 27‐kd components under non‐reducing, and 25‐ and 29‐kd components under reducing conditions. Glycosylation inhibition experiments indicate that the larger molecules represent glycosylated forms of a single protein moiety. The 27‐kd species has been purified to homogeneity (80 000‐fold enrichment) and exerts its half-maximal activity at 2 X 10(‐12) M and its maximal activity at 3 X 10(‐11) M. Antibodies prepared to purified cMGF completely neutralize the growth‐stimulating activity of the factor.

Leutz, Achim, Hartmut Beug, and Thomas Graf. “Purification and characterization of cMGF, a novel chicken myelomonocytic growth factor.” The EMBO Journal 3.13 (1984): 3191-3197.


Type II Chicken Collagen


Effects of orally administered undenatured type II collagen against arthritic inflammatory diseases: a mechanistic exploration.


Arthritis afflicts approximately 43 million Americans or approximately 16.6% of the US population. The two most common and best-known types of arthritis are osteoarthritis (OA) and rheumatoid arthritis (RA). A significant amount of scientific research has been done in attempts to explain what initiates forms of arthritis, how it is promoted and perpetuated and how to effectively intervene in the disease process and promote cartilage remodeling. Current pharmacological strategies mainly address immune suppression and anti-inflammatory mechanisms and have had limited success. Recent research provides evidence that alterations in the three-dimensional configuration of glycoproteins are responsible for the recognition/response signaling that catalyzes T-cell attack. Oral administration of autoantigens has been shown to suppress a variety of experimentally induced autoimmune pathologies, including antigen-induced RA. The interaction between gut-associated lymphoid tissue in the duodenum and epitopes of orally administered undenatured type II collagen facilitates oral tolerance to the antigen and stems systemic T-cell attack on joint cartilage. Previous studies have shown that small doses of orally administered undenatured type II chicken collagen effectively deactivate killer T-cell attack. A novel glycosylated undenatured type II collagen material (UC-II) was developed to preserve biological activity. The presence of active epitopes in the UC-II collagen is confirmed by an enzyme-linked immunosorbent assay test and distinguishes this form from hydrolyzed or denatured collagen. Oral intake of small amounts of glycosylated UC-II presents active epitopes, with the correct three-dimensional structures, to Peyer’s patches, which influences the signaling required for the development of immune tolerance. UC-II has demonstrated the ability to induce tolerance, effectively reducing joint pain and swelling in RA subjects. A pilot study was conducted for 42 days to evaluate the efficacy of UC-II (10 mg/day) in five female subjects (58-78 years) suffering from significant joint pain. Significant pain reduction including morning stiffness, stiffness following periods of rest, pain that worsens with use of the affected joint and loss of joint range of motion and function was observed. Thus, UC-II may serve as a novel therapeutic tool in joint inflammatory conditions and symptoms of OA and RA.

Bagchi, D., et al. “Effects of orally administered undenatured type II collagen against arthritic inflammatory diseases: a mechanistic exploration.” International journal of clinical pharmacology research 22.3-4 (2002): 101-110.


In Situ Hybridization Analysis of the Expression of the Type II Collagen Gene in the Developing Chicken Limb Bud


In situ hybridization with 32P- or 31S-labeled double-stranded DNA or single-stranded RNA probes was used to investigate the temporal and spatial distribution of cartilage-characteristic type II collagen mRNA during embryonic chick limb development and cartilage differentiation in vivo. When the type II collagen probes were hybridized to sections through embryonic limb buds at the earliest stages of their development (stages 18–25), an accumulation of silver grains representing type II collagen mRNA first became detectable in the proximal central core of the limb coincident with the prechondrogenic condensation of mesenchymal cells that characterizes the onset of cartilage differentiation. At later stages of development (stage 32; 7 days), intense hybridization signals with the type II collagen probes were localized over the well-differentiated cartilage rudiments, whereas few or no silver grains above background were observed over the non-chondrogenic tissues. In contrast, sections hybridized with a probe complementary to mRNA for the α1 chain of type I collagen exhibited an intense hybridization signal over the perichondrium and little or no signal over the cartilage primordia. At all stages of development examined, 32P-labeled double-stranded DNA probes or single-stranded RNA probes labeled with either 32P or 35S provided adequate hybridization signals. Several experimental protocols were employed to control for the potential cross-hybridization and non-specific hybridization of the type II collagen probes. These included the utilization of labeled noncomplementary “sense strand” type II collagen RNA as a control probe for nonspecific background and prehybridization with a large excess of appropriate unlabeled RNA to block sequences in heterologous collagen RNAs that might cross-hybridize to the specific labeled probe.

Nah, Hyun-Duck, et al. “In situ hybridization analysis of the expression of the type II collagen gene in the developing chicken limb bud.” Collagen and related research 8.4 (1988): 277-294.


Macromolecular organization of chicken type X collagen in vitro.


The macromolecular structure of type X collagen in the matrices of primary cultures of chick hypertrophic chondrocytes was initially investigated using immunoelectron microscopy. Type X collagen was observed to assemble into a mat-like structure within the matrix elaborated by hypertrophic chondrocytes. The process of self-assembly was investigated at the molecular level using purified chick type X collagen and rotary-shadowing EM. It was shown that under neutral conditions at 34 degrees C, individual type X collagen molecules associate rapidly into multimeric clusters via their carboxy-terminal globular domains forming structures with a central nodule of carboxy-terminal domains and the triple helices radiating outwards. Prolonged incubation resulted in the formation of a regular hexagonal lattice by the lateral association of the juxtaposed triple-helical domains from adjacent multimeric clusters. This extended lattice may play an important role in modifying the cartilage matrix for subsequent events occurring in endochondral bone formation.

Kwan, A. P., et al. “Macromolecular organization of chicken type X collagen in vitro.” The Journal of Cell Biology 114.3 (1991): 597-604.



Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1(V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis.


Previous work from our laboratories has demonstrated that: (a) the striated collagen fibrils of the corneal stroma are heterotypic structures composed of type V collagen molecules coassembled along with those of type I collagen, (b) the high content of type V collagen within the corneal collagen fibrils is one factor responsible for the small, uniform fibrillar diameter (25 nm) characteristic of this tissue, (c) the completely processed form of type V collagen found within tissues retains a large noncollagenous region, termed the NH2-terminal domain, at the amino end of its alpha 1 chain, and (d) the NH2-terminal domain may contain at least some of the information for the observed regulation of fibril diameters. In the present investigation, we have employed polyclonal antibodies against the retained NH2-terminal domain of the alpha 1(V) chain for immunohistochemical studies of embryonic avian corneas and for immunoscreening a chicken cDNA library. When combined with cDNA sequencing and molecular rotary shadowing, these approaches provide information on the molecular structure of the retained NH2-terminal domain as well as how this domain might function in the regulation of fibrillar structure. In immunofluorescence and immunoelectron microscopy analyses, the antibodies against the NH2-terminal domain react with type V molecules present within mature heterotypic fibrils of the corneal stroma. Thus, epitopes within at least a portion of this domain are exposed on the fibril surface. This is in marked contrast to mAbs which we have previously characterized as being directed against epitopes located in the major triple helical domain of the type V molecule. The helical epitopes recognized by these antibodies are antigenically masked on type V molecules that have been assembled into fibrils. Sequencing of the isolated cDNA clones has provided the conceptual amino acid sequence of the entire amino end of the alpha 1(V) procollagen chain. The sequence shows the location of what appear to be potential propeptide cleavage sites. One of these, if preferentially used during processing of the type V procollagen molecule, can provide an explanation for the retention of the NH2-terminal domain in the completely processed molecule. The sequencing data also suggest that the NH2-terminal domain consists of several regions, providing a structure which fits well with that of the completely processed type V molecule as visualized by rotary shadowing.

Linsenmayer, Thomas F., et al. “Type V collagen: molecular structure and fibrillar organization of the chicken alpha 1 (V) NH2-terminal domain, a putative regulator of corneal fibrillogenesis.” The Journal of Cell Biology 121.5 (1993): 1181-1189.


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