EP0206801A2
Expired / Lapsed
EP
⏱️ 0.0 years remaining
Tissue-affinitive collagen for osteogenesis and method of producing the same
Assignee: Nitta Gelatin Inc
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Filing: 1986-06-23
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Granted: —
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Expires: 2006-06-23
Abstract
Abstract A good tissue-affinity and lack of antigenicity are required for the collagen used as a carrier for BMP. Conventional collagens have these properties only insufficiently. When the tyrosine content of collagen is below 2 residues/1000 residues, the above desirable properties are exhibited. Moreover, collagens excelling in the above properties can be readily obtained by using proteolytic enzymes.
Inventors
- 👤 Masahiro Koezuka
- 👤 Kunio Takaoka
- 👤 Kaneo Suzuki
- 👤 Shigeo Yasugi
Bibliographic Details
Application Number
—
Jurisdiction
EP
Data Source
google_patents
Last Synchronized
2026-10-23 09:24
CPC Classifications
C; C07; C07K; C07K14/00; C07K14/435; C07K14/78; A; A61; A61L; A61L27/00; A61L27/14; A61L27/22; A61L27/227; A61L27/24; C07K14/475; C07K14/51; C08; C08H; C08H1/00; C08H1/06; A61F; A61F2310/00; A61F2310/00005; A61F2310/00365; A61K; A61K38/00; Y; Y10; Y10S; Y10S530/00; Y10S530/827; Y10S530/84
Claims Analysis
Total Claims: 5
Claim 1
Independent Claim
23 words
Tissue-affinitive collagen which is usable as a carrier of bone morphogenetic protein for osteogenesis,characterized by having a tyrosine content below 2 residues/1000 residues.
Claim 2
Dependent Claim
23 words
Tissue-affinitive collagen which is usable as a carrier of bone morphogenetic protein for osteogenesis,characterized by having a tyrosine content below 2 residues/1000 residues.
Claim 3
Dependent Claim
12 words
Collagen according to claim 1 whose isoelectric point is 7 or more.
Claim 4
Dependent Claim
25 words
A method of obtaining tissue-affinitive collagen as defined in claim 1 or 2, the method being characterised by subjecting aggregate-removed collagen to proteolytic enzyme action.
Claim 5
Dependent Claim
32 words
A method of obtaining tissue-affinitive collagen as defined in claim 1 or 2, the method being characterised by obtaining aggregate-removed collagen by filtration after solubilising insoluble collagen by treatment with proteolytic enzymes.
References Cited (Backward Citations)
No citation records indexed.
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