Preparation and structural analysis of actinidain-processed atelocollagen of yellowfin tuna (Thunnus albacares)

Bioscience, Biotechnology and Biochemistry

Volumn 68, Issue 4, 2004, Pages 861-867

  Morimoto, Koichi ^a   Kunii, Saori ^a   Hamano, Kaori ^a   Tonomura, Ben'ichiro ^a  

^a KINKI UNIVERSITY   (Japan)

Author keywords

Actinidain; Circular dichroism; Collagen; High performance liquid chromatography (HPLC); Triple helical structure

Indexed keywords

ACTINIDIN; ATELOCOLLAGEN; COLLAGEN; CYSTEINE PROTEINASE;

ANIMAL; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; ENZYMOLOGY; FRUIT; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROLYSIS; ISOLATION AND PURIFICATION; KIWIFRUIT; LIQUID CHROMATOGRAPHY; METABOLISM; PH; TEMPERATURE; TUNA;

ACTINIDIA; ANIMALS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CHROMATOGRAPHY, LIQUID; CIRCULAR DICHROISM; COLLAGEN; CYSTEINE ENDOPEPTIDASES; FRUIT; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; TEMPERATURE; TUNA;

ACTINIDIA DELICIOSA; SCOMBRIDAE GEN. SP.; THUNNUS; THUNNUS ALBACARES;

EID: 4544348411     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.68.861     Document Type: Article

References (38)

1. Veis, A., and George, A., Fundamentals of interstitial collagen self-assembly. In "Extracellular Matrix Assembly and Structure", eds. Yurchenco, P. D., Birk, D. E., and Mecham, R. P., Academic Press, San Diego, pp. 15-45 (1994).
2. Prockop, D. J., and Hulmes, D. J. S., Assembly of collagen fibrils de novo from soluble precursors: Polymerization and copolymerization of procollagen, pN-collagen, and mutated collagens. In "Extracellular Matrix Assembly and Structure", eds. Yurchenco, P. D., Birk, D. E., and Mecham, R. P., Academic Press, San Diego, pp. 47-90 (1994).
3. Birk, D. E., and Linsenmayer, T. F., Collagen fibril assembly, deposition, and organization into tissue-specific matrices. In "Extracellular Matrix Assembly and Structure", eds. Yurchenco, P. D., Birk, D. E., and Mecham, R. P., Academic Press, San Diego, pp. 91-128 (1994).
4. Fraser, R. D. B., Macrae, T. P., and Suzuki, E., Chain conformation in the collagen molecule. J. Mol. Biol., 129, 463-481 (1979).
5. Kadler, K. E., Hojima, Y., and Prockop, D. J., Assembly of collagen fibrils de novo by cleavage of the type I pC-collagen with procollagen C-proteinase. Assay of critical concentration demonstrates that collagen self-assembly is a classical example of an entropy-driven process. J. Biol. Chem., 262, 15696-15701 (1987).
6. Kadler, K. E., Holmes, D. F., Trotter, J. A., and Chapman, J. A., Collagen fibril formation. Biochem. J., 316, 1-11 (1996).
7. Hayashi, T., Nakamura, T., Hori, H., and Nagai, Y., The degradation rates of type I, II, and III collagens by tadpole collagenase. J. Biochem., 87, 809-815 (1980).
8. Nagai, T., Araki, Y., and Suzuki, N., Collagen of the skin of ocellate puffer fish (Takifugu rubripes). Food Chemistry, 78, 173-177 (2002).
9. Miyata, T., and Taira, T., Collagen engineering for biomaterial use. Clinical Materials, 9, 139-148 (1992).
10. Hickman, D., Sims, T. J., Miles, C. A., Bailey, A. J., de Mari, M., and Koopmans, M., Isinglass/collagen: denaturation and functionality. J. Biotechnology, 79, 245-257 (2000).
11. Ueda, H., Hong, L., Yamamoto, M., Shigeno, K., Inoue, M., Toba, T., Yoshitani, M., Nakamura, T., Tabata, Y., and Shimizu, Y., Use of collagen sponge incorporating transforming growth factor-β1 to promote bone repair in skull defects in rabbits. Biomaterials, 23, 1003-1010 (2002).
12. Ramshaw, J. A. M., Werkmeister, J. A., and Allan, B. H., Characterization of type I collagen from the skin of blue grenadier (Macruronus novaezelandiae). Arch. Biochem. Biophys., 267, 497-502 (1988).
13. Kimura, S., Miyauchi, Y., and Uchida, N., Scale and bone type I collagens of carp (Cyprinus Carpio). Comp. Biochem. Physiol., 99B, 473-476 (1991).
14. Kimura, S., Wide distribution of the skin type I collagen α3 chain in bony fish. Comp. Biochem. Physiol., 102B, 255-260 (1992).
15. Kimura, S., Omura, Y., Ishida, M., and Shirai, H., Molecular characterization of fibrillar collagen from the body wall of starfish Asterias amurensis. Comp. Biochem. Physiol., 104B, 663-668 (1993).
16. Montero, P., Alvarez, C., Martí, M. A., and Borderías, A. J., Plaice skin collagen extraction and functional properties. J. Food Sci., 60, 1-3 (1995).
17. Nagai, T., Ogawa, T., Nakamura, T., Ito, T., Nakagawa, H., Fujiki, K., Nakao, M., and Yano, T., Collagen of edible jellyfish exumbrella. J. Sci. Food Agric., 79, 855-858 (1999).
18. Nagai, T., and Suzuki, N., Isolation of collagen from fish waste material-skin, bone and fins. Food Chemistry, 68, 277-281 (2000).
19. Giraud-Guille, M. M., Besseau, L., Chopin, C., Durand, P., and Herbage, D., Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states. Biomaterials, 21, 899-906 (2000).
20. Sato, K., Ohashi, C., Muraki, M., Itsuda, H., Yokoyama, Y., Kanamori, M., Ohtsuki, K., and Kawabata, M., Isolation of intact type V collagen from fish intramuscular connective tissue. J. Food Biochem., 22, 213-225 (1998).
21. Saito, M., Takenouchi, Y., Kunisaki, N., and Kimura, S., Complete primary structure of rainbow trout type I collagen consisting of α1(I)α2(I) α3(I) heterotrimers. Eur. J. Biochem., 268, 2817-2827 (2001).
22. Arcus, A. C., Proteolytic enzyme of Actinidia chinensis. Biochem. Biophys. Acta, 33, 242-244 (1959).
23. McDowall, M. A., Anionic proteinase from Actinidia chinensis, preparation and properties of the crystalline enzyme. Eur. J. Biochem., 14, 214-221 (1970).
24. Baker, E. N., Structure of actinidin: details of the polypeptide chain conformation and active site from an electron density map at 2.8 Å resolution. J. Mol. Biol., 115, 263-277 (1977).
25. Carne, A., and Moore, C. H., The amino acid sequence of the tryptic peptides from actinidin, a proteolytic enzyme from the fruit of Actinidia chinensis. Biochem. J., 173, 73-83 (1978).
26. Brocklehurst, K., Carey, P. R., Lee, H. H., Salih, E., and Storer, A. C., Comparative resonance Raman spectroscopic and kinetic studies of acyl-enzymes involving papain, actinidin and papaya peptidase II. Biochem. J., 223, 649-657 (1984).
27. Lewis, D. A., and Luh, B. S., Development and distribution of actinidin in kiwifruit (Actinidia chinensis) and its partial characterization. J. Food Biochem., 12, 109-116 (1988).
28. Ohyama, H., Enomoto, T., and Mitsunaga, S., Variety of kiwi fruit proteases and their collagenolytic activity. Nippon Eiyo Syokuryo Gakkaishi (in Japanese), 50, 57-62 (1997).
29. Sugiyama, S., Ohtsuki, K., Sato, K., and Kawabata, M., Enzymatic properties, substrate specificities and pH-activity profiles of two kiwifruit proteases. J. Nutr. Sci. Vitaminol., 43, 581-589 (1997).
30. McDowall, M. A., The action of proteinase A2 of Actinidia chinensis on the B-chain of oxidized insulin. Biochim. Biophys. Acta, 293, 226-231 (1973).
31. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
32. 2μ fragments from mouse monoclonal antibodies of the immunoglobulin M class and characterization of the fragments. J. Immunol. Methods, 224, 43-50 (1999).
33. Hayashi, T., and Nagai, Y., Separation of the α chains of type I and III collagens by SDS-polyacrylamide gel electrophoresis. J. Biochem., 86, 453-459 (1979).
34. Brocklehurst, K., Baines, B. S., and Malthouse, J. P. G., Differences in the interactions of the catalytic groups of the active centres of actinidin and papain. Biochem. J., 197, 739-746 (1981).
35. Burjanadze, T. V., Thermodynamic substantiation of water-bridged collagen structure. Biopolymers, 32, 941-949 (1992).
36. Asahina, K., Oofusa, K., Obara, M., and Yoshizato, K., Cloning and characterization of the full length cDNA encoding α2 type I collagen of bullfrog Rana catesbeiana. Gene, 194, 283-289 (1997).
37. Helseth Jr., D. L., and Veis, A., Collagen self-assembly in vitro. Differentiating specific telopeptide-dependent interactions using selective enzyme modification and the addition of free amino telopeptide. J. Biol. Chem., 256, 7118-7128 (1981).
38. Capaldi, M. J., and Chapman, J. A., The C-terminal extrahelical peptide of type I collagen and its role in fibrillogenesis in vitro. Biopolymers, 21, 2291-2313 (1982).