| 摘要 |
Purified collagen is produced by a method containing steps of contacting a collagen sample with a first proteolytic enzyme followed by contacting with a reducing agent and a second proteolytic enzyme. Preferably, the first and second proteolytic enzymes are papain and the reducing agent is sodium sulfide, dithiothreitol, glutathionine or sodium borohydride. A biocompatible collagen is prepared by contacting the purified collagen with a delipidation agent such as chloroform or methanol to produce delipidated collagen, and then contacting the delipidated collagen with a phosphorylation agent such as sodium trimetaphosphate. Prior to phosphorylation, the delipidated collagen may be treated by compressing, dehydrating, dispersing and drying to form collagen fibers. Also, prior to phosphorylation, the delipidated collagen may be treated by filter-sterilizing. De-epithelializing of the collagen may carried out prior to treating with the first proteolytic enzyme. The purified and biocompatible collagen may be used in transplantation or hemostasis, and may be provided with compounds such as antimicrobials, antivirals, growth factors and other compounds suitable for biomedical use.
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