Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Scleroproteins – e.g. – fibroin – elastin – silk – etc.
Reexamination Certificate
1999-12-02
2001-11-27
Low, Christopher S. F. (Department: 1653)
Chemistry: natural resins or derivatives; peptides or proteins;
Proteins, i.e., more than 100 amino acid residues
Scleroproteins, e.g., fibroin, elastin, silk, etc.
C530S407000, C530S412000, C435S212000, C435S273000, C514S002600
Reexamination Certificate
active
06323319
ABSTRACT:
FIELD OF THE INVENTION
The present invention relates to a method of preparing hydrolyzed collagen type II and its use as a therapeutic agent and nutritional supplement.
BACKGROUND OF THE INVENTION
Collagen is a complex structural protein which provides strength and flexibility to skin, hair and nails. Collagen is an essential and major component of muscles, tendons, cartilage, ligaments, joints and blood vessels. There are three main types of collagen: I, II and III. Types I and III are primarily found in skin, tendon and bone. In contrast, type II is found predominantly in particular cartilage. Collagen is an unusual protein, in that the proportion of glycine residues is nearly one-third which is unusually high. Proline is also present to a much greater extent in collagen than in most other proteins. Moreover, collagen contains two amino acids, 4-hydroxyproline and 5-hydroxylysine, that are found in very few other proteins. The amnino acid sequence of collagen is remarkably regular, nearly every third amino acid being glycine. In addition, the sequence glycine-proline-hydroxyproline recurs frequently. In contrast, globular proteins rarely exhibit regularities in their amino acid sequences (Stryer, L.,
Biochemistry
, Third Edition, W. H. Freeman and Co., New York, 1.988, pp. 262).
In 1986, collagen was sold for the first time in the United States for use as a food supplement Collagen (a mixture of Types I, II) was extracted from calf skin tissue, hydrolyzed and prepared in powdered form for use as a dietary supplement. The composition was sold under the name “Hydrolyzed Collagen Beauty Supplement™” (Smarter Nails & Hair, Inc., Newport Beach, Calif.). In 1987, “Hydrolyzed, Collagen Beauty Supplement Tablet™” (Smarter Nails & Hair, Inc., Newport Beach, Calif.) was sold which comprised collagen powder and 10 mg vitamin C compressed into 1,000 mg tablets.
U.S. Pat. No. 4,804,745 to Koepff et al. discloses agents containing collagen peptides produced by enzymatic hydrolysis for the treatment of degenerative joint diseases. These peptides can be obtained from animal skin, animal bones and other sufficiently purified connective tissue and have average molecular weights of between 30 and 45 kilodaltons.
U.S. Pat. No. 5,399,347 to Trentham et al. and Trentham et al. (
Science
261:1727-1729, 1993) disclose the effective treatment of rheumatoid arthritis (RA) with water-soluble whole chick collagen type II or biologically active peptides derived therefrom. The mechanism by which the effect is believed to occur is via oral tolerization to autoantigens.
U.S. Pat. No. 5,364,845 to Henderson discloses a therapeutic composition and method for the protection, treatment and repair of connective tissue in mammals. This composition comprises glucosamine, chondroitin sulfate and manganese ascorbate. U.S. Pat. No. 5,587,363 to Henderson discloses a therapeutic composition and method for the protection, treatment and repair of connective tissue in mammals which includes aminosugars and glycosaminoglycans.
There is a constant need for compositions capable of promoting repair of damaged connective tissue. The present invention addresses this need.
SUMMARY OF THE INVENTION
One embodiment of the present invention is hydrolyzed collagen type II, the hydrolyzed collagen having an average molecular weight of between about 1,500 and 2,500 daltons. Preferably, the hydrolyzed collagen type II has an average molecular weight of about 1,800 daltons. In one aspect of this preferred embodiment, the collagen is obtained from chicken sternal cartilage.
The present invention also provides a method of inducing cartilage formation in an individual with a connective tissue disorder, comprising orally administering to the individual an effective daily cartilage-inducing amount of hydrolyzed collagen type II. The connective tissue disorder includes degenerative joint diseases, joint defects, osteoarthritis, polychondritis, vascular disease and cartilage injuries. Preferably, the effective daily amount is between about 500 and 5,000 mg. More preferably, the effective daily amount is between about 1,000 and 4,000 mg. Most preferably, the effective daily amount is between about 2,000 and 3,000 mg.
Another embodiment of the invention is a method of providing collagen type II as a nutritional supplement, comprising orally administering to an individual a daily dosage of hydrolyzed collagen having an average mole weight of between about 1,500 and 2,500 daltons.
Still another embodiment of the invention is a method of preparing hydrolyzed collagen type II powder, comprising the following steps: cutting fresh chicken sternal cartilage to within not less than about 2 mm of the bone; suspending tho cartilage in an aqueous solution; treating said cartilage with a proteolytic enzyme to form a hydrolysate; sterilizing the hydrolysate; filtering the hydrolysate; concentrating the hydrolysate; and drying the hydrolysate to form a collagen type II powder. The method may further comprise the step of freezing the cartilage after the cutting step. Preferably, the aqueous solution is water. Advantageously, the enzyme is papain, ficin or bromelain. In one aspect of this preferred embodiment, the sterilizing step comprises heating the hydrolysate at 95° C. for about 30 minutes. Preferably, the drying step comprises spray drying. Preferably, the pH of the suspending and treating steps is between about 4 and 8.
REFERENCES:
patent: 4511653 (1985-04-01), Play et al.
patent: 4804745 (1989-02-01), Koepff et al.
patent: 5206023 (1993-04-01), Hunziker et al.
patent: 5364775 (1994-11-01), Katsumata et al.
patent: 5364845 (1994-11-01), Henderson
patent: 5399347 (1995-03-01), Trentham et al.
patent: 5587363 (1996-12-01), Henderson
patent: 5645851 (1997-07-01), Moore
patent: WO 97/254435 (1997-07-01), None
Barinaga, Treating Arthritis With Tolerance,Science261:1669-1670 (1993).
Bedi et al., Purification and characterization of a collagen-degrading protease fromPorphyromonas gingivalis, J. Biol. Chem. 269:599-606 (1994).
Brucknet et al.,p-HMW-Collegen, a minor collagen obtained from chick embryo cartilage without proteolytic treatment of the tissue, Eur. J. Biochem.
Cremer et al.,Collagen-Induced Arthritis in Rats: Antigen-Specific Suppression of Arthritis and Immunity By Intravenously Injected Native Type II Collagen, J. of Immun. 131(6):2995-3000 (1983).
Darnell et al.,Molecular Cell Biology, Scientific American Books, Inc. New York, NY 1986.
Englert et al., Suppression of Type II Collagen-Induced Arthritis by the Intravenous Adminstration of Type II Collagen or Its Constituent Peptide á1(II)CB10,Cellular Immunology87:357-365 (1984).
Fawcett,A textbook of Histology, W.B. Ssaunders Co. Philadelphia, PA (1986).
File Caplus on STN: No. 1984:180121. RO 80226, Nov. 30, 1982 Abstract only.
Knauper et al., Biochemical characterization of human collagenase-3,J. Biol. Chem. 271:1544-1550 (1996).
New Product Advertisement for “Hydrolyzed Collagen Beauty Supplement”, Smarter Nails & Hair, Inc., Newport Beach, CA 92660 (1987).
Stryer, Collagen Has An Unusual Amino Acid Composition And Sequence,Biochemistry, Third Edition, W.H. Freeman and Co., New York, p. 262 1988).
Trentham, et al., Autoimmunity to Type II Collagen: An Experimental Model of Arthritis,J. of Exp. Medicine146:857-868 (1977).
Trentham, et al., Effects of Oral Administration of Type II Collagen on Rheumatoid Arthritis,Science261:1727-1730 (1993).
Five Continent Enterprise, Inc.
Gupta Anish
Low Christopher S. F.
Stetina Brunda Garred & Brucker
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