Purification and characterization of a serine protease (CPM-2) with fibrinolytic activity from the dung beetles

Archives of Pharmacal Research

Volumn 28, Issue 7, 2005, Pages 816-822

  Mi, Young Ahn ^a   Hahn, Bum Soo ^a   Kang, Sun Ryu ^a   Jae, Sam Hwang ^a   Yeong, Shik Kim ^b  

^a National Institute of Animal Science   (South Korea)

^b Seoul National University   (South Korea)

Author keywords

Catharsius molossus; Catharsius protease (CPM 2); Fibrinolytic activity

Indexed keywords

DIVALENT CATION; FIBRIN DEGRADATION PRODUCT; FIBRINOGEN; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

AMINO ACID SEQUENCE; ANIMAL; ARTICLE; BEETLE; ENZYMOLOGY; FIBRINOLYSIS; IN VITRO STUDY; ISOLATION AND PURIFICATION; METABOLISM; PH; TEMPERATURE;

AMINO ACID SEQUENCE; ANIMALS; BEETLES; CATIONS, DIVALENT; FIBRIN FIBRINOGEN DEGRADATION PRODUCTS; FIBRINOGEN; FIBRINOLYSIS; HYDROGEN-ION CONCENTRATION; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; TEMPERATURE;

EID: 30544449142     PISSN: 02536269     EISSN: 02536269     Source Type: Journal    
DOI: 10.1007/BF02977348     Document Type: Article

References (16)

1. Ahn, M. Y., Hahn, B. S., Ryu, K. S., and Cho, S. I., Effects of insect crude drugs on blood coagulation and fibrinolysis system. Natural Product Sciences, 8, 66-70 (2002).
2. Ahn, M. Y., Hahn, B. S., Ryu, K. S., Kim, J. W., Kim, I., and Kim, Y. S., Purification and characterization of a serine protease with fibrinolytic activity from the dung beetles, Catharsius molossus. Thrombosis Res., 112, 339-347 (2003).
3. Astrup, T. and Müllertz, S., The fibrin plate method for estimating of fibrinolytic activity. Arch. Biochem. Biophys., 40, 346-351 (1952).
4. Beynon, R. J. and Kay, J., The inactivation of native enzymes by a neutral proteinase from rat intestinal muscle. Biochem. J., 173, 291-298 (1978).
5. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese bovine insulin. Biochemistry, 6, 215-224 (1967).
6. Collen, D. and Lijnen, H. R., Basic and clinical aspects of fibrinolysis and thrombolysis. Blood ,78, 3114-3124 (1991)
7. Dametto, M., David, A. P., Azzolini, S. S., Campos, I. T. N., Tanaka, A. M., Gomes, A., Andreotti, R., and Tanaka, A. S., Purification and characterization of a trypsin-like enzyme with fibrinolytic activity present in the abdomen of horn fly, Haematobia irritans (Diptera: Muscidae). J. Protein Chem., 19, 515-521 (2000).
8. Francis, C. W., Marder, V. J., and Barlow, G. H., Plasmic degradation of cross-linked fibrin: Characterization of new macromolecular soluble complexes and model of their structure. J. Clin. Invest., 66, 1033-1043 (1980).
9. Fujita, M., NoMura, K., Hong, K., Ito, Y., Asada, A., and Nishimura, S., Purification and characterization of a strong fibrinolytic enzyme (nattokinase) in the vegetable cheese natto, a popular soybean fermented food in Japan. Biochem. Biophys. Res. Commun., 197, 1340-1347 (1993).
10. Hahn, B. S., Cho, S. Y., Ahn, M. Y., and Kim, Y. S., Purification and characterization of a plasmin-like protease from Tenodera sinensis (Chinese mantis). Insect Biochem. Mol. Biol., 31, 573-581 (2001).
11. Hahn, B. S., Cho, S. Y., Wu, S. J., Chang, I. M., Baek, K. H., Kim, Y. C., and Kim, Y. S., Purification and characterization of a serine protease with fibrinolytic activity from Tenodera sinensis (Chinese mantis). Biochim. Biophys. Acta, 1430, 376-386 (1999).
12. Hahn, B. S., Yang, K. Y., Park, E. M., Chang, I. M., and Kim, Y. S., Purification and molecular cloning of a thrombin-like enzyme from Agkistrodon caliginosus (The Korean viper). J. Biochem. (Tokyo), 119, 835-843 (1996).
13. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
14. Nakajima, N., Mihara, H., and Sumi, H., Characterization of potent fibrinolytic enzymes in earthworm, Lumbricus rubellus. Biosci. Biotech. Biochem., 57, 1726-1730 (1993).
15. Ouriel, K., Current status of thrombolysis for peripheral arterial occlusive disease. Ann. Vas. Surg., 16, 797-804 (2002).
16. Williams, K., Neice, R. L., Aterton, D., Fowler, A. V., Kutny, K., and Smith, A. J., The size, operation and technical capabilities of protein and nucleic acid core facilities. FASEB J., 2, 3124-3130 (1998).