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US4389487A Expired / Lapsed US ⏱️ 0.0 years remaining

Process for the preparation of a collagen product for medical and cosmetic purposes

Assignee: DSM Nutritional Products AG
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Filing: 1980-09-17
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Granted: 1983-06-21
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Expires: 2000-09-17
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Abstract

Abstract PCT No. PCT/CH80/00107 Sec. 371 Date Jun. 8, 1981 Sec. 102(e) Date May 29, 1981 PCT Filed Sep. 17, 1980 PCT Pub. No. WO81/00963 PCT Pub. Date Apr. 16, 1981.Process for the preparation of collagen products for medical and cosmetic purposes, wherein collagen products prepared according to the method described in U.S. Pat. No. 4,066,083 are subjected to an additional heat treatment or a treatment with gaseous hydrogen halide in order to improve the physicochemical and mechanical properties of the collagen product, in particular its absorption and mechanical strength.

Inventors

  • 👤 Peter E. Ries

Bibliographic Details

Application Number —
Jurisdiction US
Data Source google_patents
Last Synchronized 2026-10-23 05:29
CPC Classifications
C; C07; C07K; C07K14/00; C07K14/435; C07K14/78; A; A61; A61K; A61K8/00; A61K8/18; A61K8/30; A61K8/64; A61K8/65; A61Q; A61Q19/00; C08; C08H; C08H1/00; C08H1/06; C09; C09H; C09H1/00; A61K38/00; Y; Y10; Y10S; Y10S128/00; Y10S128/08

Claims Analysis

Total Claims: 8
Claim 1
Independent Claim 348 words
In a process for the preparation of collagen products for medical and cosmetic purposes comprising the steps of finely comminuting collagen-containing animal tissues at temperatures not exceeding 40° C., degreasing the resulting tissue pulp and simultaneously removing therefrom undesireable water-soluble non-collagen type ballast substances by repeatedly treating the said tissue pulp with about a five-fold volume, based on the pulp volume, of a 5 to 15% aqueous sodium chloride solution containing about 0.2 to 1 part by weight of sodium azide as a preserving agent per 1000 parts by weight of the said solution and 0.5 to 2% by weight of a non-ionic fat-dispersing wetting agent, washing the resulting fiber pulp with water or 0.1 to 0.5% aqueous formic, acetic or citric acid, digesting the fiber pulp for 8 to 48 hours at a pH of about 2.5 to 3.5 in a five-fold volume, based on the volume of the pulp, of 0.1 to b 5% aqueous acetic acid containing about 1 part by weight of pepsin per 1000 parts by weight of the tissue used as the starting material in order to remove non-collagen type proteins and telopeptides, precipitating collagen from the resulting collagen suspension by the addition thereto of aqueous sodium chloride in such a quantity that the sodium chloride concentration of the suspension is about 3 to 5%, separating the precipitated collagen and substantially desalting it by ultrafiltration, dialysis or washing with 60 to 75% aqueous ethyl alcohol so that the collagen concentration in the desalted solution is about 1%, dissolving the desalted collagen in demineralized or distilled water containing up to 3% by weight of a volatile strong organic acid in such a proportion that the concentration of collagen in the resulting solution corresponds to a dry residue of about 0.5 to 2% by weight, freeze-drying the collagen solution, and sterilizing the freeze-dried collagen product, the improvement comprising: subjecting the collagen product to a heat treatment or a treatment with gaseous hydrogen halide after freeze-drying, before or after sterilization, for a time sufficient to impart increased absorption and wet strength to the collagen product.
Claim 2
Dependent Claim 348 words
In a process for the preparation of collagen products for medical and cosmetic purposes comprising the steps of finely comminuting collagen-containing animal tissues at temperatures not exceeding 40° C., degreasing the resulting tissue pulp and simultaneously removing therefrom undesireable water-soluble non-collagen type ballast substances by repeatedly treating the said tissue pulp with about a five-fold volume, based on the pulp volume, of a 5 to 15% aqueous sodium chloride solution containing about 0.2 to 1 part by weight of sodium azide as a preserving agent per 1000 parts by weight of the said solution and 0.5 to 2% by weight of a non-ionic fat-dispersing wetting agent, washing the resulting fiber pulp with water or 0.1 to 0.5% aqueous formic, acetic or citric acid, digesting the fiber pulp for 8 to 48 hours at a pH of about 2.5 to 3.5 in a five-fold volume, based on the volume of the pulp, of 0.1 to b 5% aqueous acetic acid containing about 1 part by weight of pepsin per 1000 parts by weight of the tissue used as the starting material in order to remove non-collagen type proteins and telopeptides, precipitating collagen from the resulting collagen suspension by the addition thereto of aqueous sodium chloride in such a quantity that the sodium chloride concentration of the suspension is about 3 to 5%, separating the precipitated collagen and substantially desalting it by ultrafiltration, dialysis or washing with 60 to 75% aqueous ethyl alcohol so that the collagen concentration in the desalted solution is about 1%, dissolving the desalted collagen in demineralized or distilled water containing up to 3% by weight of a volatile strong organic acid in such a proportion that the concentration of collagen in the resulting solution corresponds to a dry residue of about 0.5 to 2% by weight, freeze-drying the collagen solution, and sterilizing the freeze-dried collagen product, the improvement comprising: subjecting the collagen product to a heat treatment or a treatment with gaseous hydrogen halide after freeze-drying, before or after sterilization, for a time sufficient to impart increased absorption and wet strength to the collagen product.
Claim 3
Dependent Claim 32 words
The process according to claim 1 which comprises subjecting the freeze-dried collagen product to temperatures of 80° to 150° C. for 1/4 to 12 hours and sterilizing the collagen product by irradiation.
Claim 4
Dependent Claim 23 words
The process according to claim 1 which comprises subjecting the freeze-dried collagen product to a hydrogen halide atmosphere for 1 to 60 minutes.
Claim 5
Dependent Claim 15 words
The process according to claim 1 which comprises using pig skin as the animal tissue.
Claim 6
Dependent Claim 15 words
The process according to claim 1 which comprises using bovine tendons as the animal tissue.
Claim 7
Dependent Claim 23 words
The process according to claim 1 which comprises subjecting the freeze-dried collagen product to a hydrogen chloride atmosphere for 1 to 60 minutes.
Claim 8
Dependent Claim 39 words
An improved collagen product, having a felt-, sponge- or fleece-like structure, obtained by the process according to one of claims 1, 2,3, 4, 5 or 6, wherein the improvement comprises increased absorption and wet strength of the collagen product.

References Cited (Backward Citations)

CA585232A Cited
CA665262A Cited
DE673203C Cited
DE1692548U Cited
GB1144552A Cited
US3303038A Cited
US3664844A Cited
FR2108068B1 Cited
DE2625289A1 Cited
US4066083A Cited
FR2369329B1 Cited

USPTO Annuity & Maintenance Windows

Annuity Stage Window Opens Payment Deadline Surcharge Period Until Estimated Fee Status
3.5 Years (Year 4) 1986-06-20 1986-12-20 1987-06-21 $2000.00 Window Closed / Lapsed
7.5 Years (Year 8) 1990-06-20 1990-12-20 1991-06-21 $3760.00 Window Closed / Lapsed
11.5 Years (Year 12) 1994-06-20 1994-12-20 1995-06-21 $7700.00 Window Closed / Lapsed

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