Research On The Biocompatibility Of Tilapia Collagen

Collagen is one of the most abundant protein in the mammals, it accounts for about 25% ~ 33% of total protein in bodies, and play an important part in the composition and procession of interstitial cells. It is also widely exists in the animal’s skin, bone, cartilage, teeth, tendons, ligaments and blood vessels, with the important effect of support organ and protect bodies. It has quite good application prospect in many areas because of characteristics diversity and complexity of its structure and function. There are 3 common kind of collagen with type I, typeⅡ and typeⅢ collagen. TypeⅠcollagen is the main collagen in the adult animal skins. The content of typeⅠcollagen in fish is higher than that of land animals, especially in the skin and bones. The molecular structure of typeⅠcollagen is stable and has good ability of biocompatibility, biodegradability and bioactive. But with type I collagen used in biomedical more and more widely, biological compatibility is becoming a serious problem. As a foreign rejection materials for the host, is usually bound to generate a response in the body. In order to make a further study of the biocompatibility in mammals influenced by type I collagen extracted from fish,, to find out the possibility of its application in the biomedical., We deeply analyzed the biocompatibility of fish sourced of type I collagen, enriched the its application functions in biomedical field, fill in the research blank of the biological compatibility of fish sourced type I collagen.ChapterⅠintroduces the research background, including the source of fish collagen, characteristics research progress of collagen structure, biochemical characteristics of research methods and the biocompatibility evaluation method of type I collagen.Chapter Ⅱanalyzes the biochemical characteristics of tilapia collagen.Tilapia collagen was extracted by gastric-protein restriction enzymes separation method and acetic acid solution method respectively. protein molecules was measured by SDS-polyacrylamide gel electrophoresis(SDS-PAGE). SDS-PAGE showed that tilapia collagen is composed by 2 α-chains which the molecular mass is about 130 k D and 1 of β-chain which molecular mass was about 116 k D. Using scanning electron microscopy(sem) to observe the three-dimensional structure of the tilapia collagen characteristics, analysis of the collagen fiber superhelix structure and stretch structure. The denaturation temperature, secondary structure characteristic and the infrared spectrum characteristic were analyzed by differential scanning calorimetry, round two chromatography, infrared spectroscopy respectively.ChapterⅢ discusses the tilapia collagen acute systemic toxicity.Observe the characteristics change of cardiovascular system, respiratory system, sports system, nervous system, feeling, body weight changes and organ after the death of animal by acute systemic toxicity test. The results show that all groups of mice with no death occurred phenomenon, movement is normal, not found difficulty breathing, abdominal stimulation and without any toxic symptoms. Weight and viscera index showed that there is no acute systemic toxicity in mice. There is no obvious pathophysiological in experimental animals caused by tilapia collagen.ChapterⅣdiscussed the tilapia collagen immune features.The present study was deals with the antigenicity of TypeⅠcollagen isolated from Tilapia skin and evaluated the biocompatibility of TypeⅠcollagen. Methods: The purity of Tilapia skin collagen was confirmed by SDS-PAGE, and the antigenicity was evaluated by changes in the antibody such as Ig G, Ig A and Ig M induced by Tilapia skin TypeⅠcollagen in ICR mouse model using ELISA. Results: Results indicated that the Tilapia skin Type I collagen was pure. The antibody concentration of the Tilapia skin collagen immunized mice was 160.50-164.25μg/L, and the concentration of Ig G, Ig A and Ig M were 421.79-433.72ng/m L, 46.52-50.33μg/m L, 1.80-1.93ng/m L. Conclusions: Tilapia skin typeⅠcollagen present weaker antigen and proved the superior biocompatibility for biomedical applications.Chapter Ⅴ further discusses the blood compatibility of tilapia collagen.Hemolysis test were conducted by ear vein blood of New Zealand white rabbit. After the preparation of cell suspension and tilapia type I collagen extract fusion, the blood compatibility of tilapia collagen levels were tested.