Tanaka, Teruyoshi
(Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
,
Takahashi, Kenji
(Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
,
Tsubaki, Kazufumi
(ADEKA Corporation)
,
Hirata, Maika
(Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
,
Yamamoto, Keiko
(Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
,
Biswas, Amal
(Aquaculture Research Institute, Uragami Station, Kindai University)
,
Moriyama, Tatsuya
(Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
,
Kawamura, Yukio
(Department of Applied Biological Chemistry, Graduate School of Agriculture, Kindai University)
In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturati...
In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.
In this study, we isolated and characterized the acid-soluble skin collagen of Pacific bluefin tuna (PBT, Thunnus orientalis). The PBT skin collagen was composed of two ${\alpha}$ chains (${\alpha}1$ and ${\alpha}2$) and one ${\beta}$ chain. The denaturation temperature of PBT collagen was low although it was rich in proline and hydroxyproline. The primary structure of PBT skin collagen was almost identical to that of calf and salmon skin collagen; however, it differed with respect to the epitope recognition of the antibody against salmon type I collagen. These results suggest that the primary structure of skin collagen was highly conserved among animal species, although partial sequences that included the epitope structure differed among collagens.
* AI 자동 식별 결과로 적합하지 않은 문장이 있을 수 있으니, 이용에 유의하시기 바랍니다.
제안 방법
Although the PBT skin collagen may contain the α3 chain, its presence was not determined using ion exchange chromatographyin this study.
The skin was dissected from the body and stored at − 20 °C. Bluefin tuna skin collagen was isolated using a previously reported procedure (Han et al., 2011) with slight modifications. All steps of the extraction was performed at 4 °C.
Peptide mapping was performed to compare the primary structure of PBT skin collagen with calf and salmon skin collagen. The electrophoretic patterns of lysyl endopeptidase-digested PBT, calf, and salmon skin collagen were observed on a 7.
후속연구
The primary structure of PBT skin collagen was approximately identical to that of calf and salmon skin collagen; however, it varied from the others with respect to epitope recognition of the antibody against salmon type I collagen. Further studies are required for understanding the specific primary or higher-order structure of PBT collagen.
Therefore, epitope recognition by anti-collagen antibody might differ among tuna species. However, further studies are required to understand its structural integrity.
참고문헌 (38)
Arnesen JA, Gildberg A. Extraction and characterisation of gelatine from Atlantic salmon (Salmo salar) skin. Bioresour Technol. 2007;98:53-7.
Dion AS, Myers JC. COOH-terminal propeptides of the major human procollagens: structural, functional and genetic comparisons. J Mol Biol. 1987;193:127-43.
Dong X, Yuan Q, Qi H, Yang J, Zhu B, Zhou D, Murata Y, Ye W. Isolation and characterization of pepsin-soluble collagen from abalone (Haliotis discus hannai) gastropod muscle part II. Food Sci Technol Res. 2012;18:271-8.
Giraud-Guille MM, Besseau L, Chopin C, Durand P, Herbage D. Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states. Biomaterials. 2000;21:899-906.
Gomez-Guillen MC, Turnay J, Fernandez-Diaz MD, Ulmo N, Lizarbe MA, Montero P. Structural and physical properties of gelatin extracted from different marine species: a comparative study. Food Hydrocoll. 2002;16:25-34.
Han SH, Uzawa Y, Moriyama T, Kawamura Y. Effect of collagen and collagen peptides from bluefin tuna abdominal skin on cancer cells. Health. 2011;3:129-34.
Hwang JH, Mizuta S, Yokoyama Y, Yoshinaka R. Purification and characterization of molecular species of collagen in the skin of skate (Raja kenojei). Food Chem. 2007;100:921-5.
Hwang JH, Yokoyama Y, Mizuta S, Yoshinaka R. cDNA cloning and characterization of type I procollagen ${\alpha}1$ chain in the skate Raja Kenojei. Comp Biochem Physiol B: Biochem Mol Biol. 2006;144:1-10.
Kaji T, Tanaka M, Takahashi Y, Oka M, Ishibashi N. Preliminary observations on development of Pacific bluefin tuna Thunnus thynnus (Scombridae) larvae reared in the laboratory, with special reference to the digestive system. Mar Freshw Res. 1996;47:261-9.
Kittiphattanabawon P, Benjakul S, Visessanguan W, Nagai T, Tanaka M. Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus). Food Chem. 2005;89:363-72.
Kobayashi Y, Huge J, Imamura S, Hamada-Sato N. Study of the cross-reactivity of fish allergens based on a questionnaire and blood testing. Allergol Int. 2016;65:272-9.
Laemmli UK. Cleavage of structural proteins during assembly of head bacterriophage T4. Nature. 1970;277:680-5.
Miyashita S, Kato K, Sawada Y, Murata O, Ishitani Y, Shimizu K, Yamamoto S, Kumai H. Development of digestive system and digestive enzyme activity of larval and juvenile bluefin tuna, Thunnus thynnus, reared in the laboratory. Aquac Sci. 1998;46:111-20.
Miyashita S, Sawada Y, Okada T, Murata O, Kumai H. Morphological development and growth of laboratory-reared larval and juvenile Thunnus thynnus (Pisces: Scombridae). Fish Bull. 2001;99:601-16.
Muyonga JH, Cole CGB, Doudu KG. Charaterisation of acid soluble collagen from skins of young and adult nile perch (Lates niloticus). Food Chem. 2004;85:81-9.
Muyonga JH, Cole CGB, Duodu KG. Fourier transform infrared (FTIR) spectroscopic study of acid soluble collagen and gelatin from skins and bones of young and adult Nile perch (Lates niloticus). Food Chem. 2004;86:325-32.
Nagai T, Suzuki N, Tanoue Y, Kai N, Nagashima T. Characterization of acid-soluble collagen from skins of surf smelt (Hypomesus pretiosus japonicus Brevoort). Food Nutr Sci. 2010;1:59-66.
Nalinanon S, Benjakul S, Visessanguan W, Kishimura H. Use of pepsine for collagen extraction from the skin of bigeye smapper (Priacanthus tayenus). Food Chem. 2007;104:591-601.
Nomura Y, Sakai H, Ishii Y, Shirai K. Preparation and some properties of type I collagen from fish scales. Biosci Biotechnol Biochem. 1996;60:2092-4.
Payne KJ, Veis A. Fourier transform IR spectroscopy of collagen and gelatin solutions: deconvolution of the amide I band for conformational studies. Biopolymers. 1988;27:1749-60.
Piez KA. Characterization of a collagen from codfish skin containing three chromatographically different ${\alpha}$ chains. Biochemistry. 1965;4:2590-6.
Ramshaw JA, Shah NK, Brodsky B. Gly-X-Y tripeptide frequencies in collagen: a context for host-guest triple-helical peptides. J Struct Biol. 1998;122:86-91.
Saito M, Takenouchi Y, Kunisaki N, Kimura S. Complete primary structure of rainbow trout type I collagen consisting of ${\alpha}1$ (I) ${\alpha}2$ (I) ${\alpha}3$ (I) heterotrimers. FEBS J. 2001;268:2817-27.
Sawada Y, Okada T, Miyashita S, Murata O, Kumai H. Completion of the Pacific bluefin tuna Thunnus orientalis (Temminck et Schlegel) life cycle. Aquac Res. 2005;36:413-21.
Senaratne LS, Park PJ, Kim SK. Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin. Bioresour Technol. 2006;97:191-7.
Takii K, Miyashita S, Seoka M, Tanaka Y, Kubo Y, Kumai H. Changes in chemical contents and enzyme activities during embryonic development of bluefin tuna. Fish Sci. 1997;63:1014-8.
Tanaka T, Takahashi K, Adachi K, Ohta H, Yoshimura Y, Agawa Y, Zaima N, Moriyama T, Kawamura Y. Molecular cloning and expression profiling of procollagen ${\alpha}1$ (I) of cultured Pacific bluefin tuna. Fish Sci. 2014;80:603-12.
Tanaka T, Takahashi K, Iwamoto N, Agawa Y, Sawada Y, Yoshimura Y, Zaima N, Moriyama T, Kawamura Y. Hepatoprotective action of dietary bluefin tuna skin proteins on $CCl_{4}$ -intoxicated mice. Fish Sci. 2012;78:911-21.
Tanaka Y, Gwak WS, Tanaka M, Sawada Y, Okada T, Miyashita S, Kumai H. Ontogenetic changes in RNA, DNA and protein contents of laboratory-reared Pacific bluefin tuna Thunnus orientalis. Fish Sci. 2007;73:378-84.
Wong DWS. Mechanism and theory in food chemistry. New York: Van Nostrand Reinhold; 1989.
YataM, Yoshida C, Fujisawa S, Mizuta S, Yoshinaka R. Identification and characterization of molecular species of collagen in fish skin. J Food Sci. 2001;66:247-51.
Zhang M, Liu WT, Li GY. Isolation and characterization of collagens from the skin of largefin longbarbel catfish (Mystus Macropterus). Food Chem. 2009;115:826-31.
Zhang X, Azuma N, Hagihara S, Adachi S, Ura K, Takagi Y. Characterization of type I and II procollagen ${\alpha}1$ chain in Amur sturgeon (Acipenser schrenckii) and comparison of their gene expression. Gene. 2016;579:8-16.
※ AI-Helper는 부적절한 답변을 할 수 있습니다.