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Volumn 84, Issue 4, 1997, Pages 307-312

Purification and characterization of a novel fibrinolytic enzyme from Bacillus sp. KA38 originated from fermented fish

Author keywords

Bacillus; Fermented fish; Fibrinolytic enzyme

Indexed keywords

AMINO ACIDS; BACTERIA; BIODEGRADATION; CATALYST ACTIVITY; CATALYST SELECTIVITY; COLUMN CHROMATOGRAPHY; ELECTROPHORESIS; FERMENTATION; FRACTIONATION; MOLECULAR WEIGHT; ORGANOMETALLICS; PURIFICATION;

EID: 0031442243     PISSN: 0922338X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0922-338X(97)89249-5     Document Type: Article
Times cited : (110)

References (24)
  • 1
    • 0004053611 scopus 로고
    • John Wiley & Sons, New York
    • Voet, D. and Voet, J. G.: Biochemistry, p. 1087-1095. John Wiley & Sons, New York (1990).
    • (1990) Biochemistry , pp. 1087-1095
    • Voet, D.1    Voet, J.G.2
  • 2
    • 0020064684 scopus 로고
    • Isolation and characterization of urokinase from human plasma
    • Wun, T. C., Schleuning, W. D., and Reich, E.: Isolation and characterization of urokinase from human plasma. J. Biol. Chem., 257, 3276-3283 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 3276-3283
    • Wun, T.C.1    Schleuning, W.D.2    Reich, E.3
  • 4
    • 0029123464 scopus 로고
    • Production and properties of fibrinolytic enzyme in solid state cultures of Fusarium pallidoroseum
    • El-Aassar, S. A.: Production and properties of fibrinolytic enzyme in solid state cultures of Fusarium pallidoroseum. Biotechnol. Lett., 17, 943-948 (1995).
    • (1995) Biotechnol. Lett. , vol.17 , pp. 943-948
    • El-Aassar, S.A.1
  • 5
    • 0029079778 scopus 로고
    • Identification of plasminogen binding region in streptokinase that is necessary for the creation of functional streptokinase-plasminogen activator complex
    • Reed, G. L., Lin, L. F., Parhami-Seren, B., and Russie, P.: Identification of plasminogen binding region in streptokinase that is necessary for the creation of functional streptokinase-plasminogen activator complex. Biochemistry, 34, 10266-10271 (1995).
    • (1995) Biochemistry , vol.34 , pp. 10266-10271
    • Reed, G.L.1    Lin, L.F.2    Parhami-Seren, B.3    Russie, P.4
  • 7
    • 0030055048 scopus 로고    scopus 로고
    • Domain structure, stability and interactions in streptokinase
    • Medved, L. V., Solovjov, D. A., and Ingham, K. C.: Domain structure, stability and interactions in streptokinase. Eur. J. Biochem., 239, 333-339 (1996).
    • (1996) Eur. J. Biochem. , vol.239 , pp. 333-339
    • Medved, L.V.1    Solovjov, D.A.2    Ingham, K.C.3
  • 9
    • 0020602912 scopus 로고
    • Activation of plasma fibrinolysis after intrarectal administration of high molecular weight urokinase and its derivative
    • Sumi, H., Maruyama, M., Yoneta, T., and Mihara, H.: Activation of plasma fibrinolysis after intrarectal administration of high molecular weight urokinase and its derivative. Acta Haematol., 70, 289-295 (1983).
    • (1983) Acta Haematol. , vol.70 , pp. 289-295
    • Sumi, H.1    Maruyama, M.2    Yoneta, T.3    Mihara, H.4
  • 10
    • 0021892750 scopus 로고
    • The transport of 125I-labeled human high molecular weight urokinase across the intestinal tract in a dog model with stimulation of synthesis and/or release of plasminogen activators
    • Sasaki, K., Moriyama, S., Sumi, H., Toki, N., and Robbins, K. C.: The transport of 125I-labeled human high molecular weight urokinase across the intestinal tract in a dog model with stimulation of synthesis and/or release of plasminogen activators. Blood, 66, 67-75 (1985).
    • (1985) Blood , vol.66 , pp. 67-75
    • Sasaki, K.1    Moriyama, S.2    Sumi, H.3    Toki, N.4    Robbins, K.C.5
  • 11
    • 0344250238 scopus 로고
    • Shift of fibrinolysis system at oral administration of urokinase in human subjects: Double blind cross over study
    • in Japanese
    • Abe, T., Kazama, M., Kinoshita, T., Naito, I., Ogushi, T., Yoshimura, Y., Teruya, J., and Shimizu, N.: Shift of fibrinolysis system at oral administration of urokinase in human sub- jects: double blind cross over study. Blood Vessels, 13, 472-479 (1982). (in Japanese)
    • (1982) Blood Vessels , vol.13 , pp. 472-479
    • Abe, T.1    Kazama, M.2    Kinoshita, T.3    Naito, I.4    Ogushi, T.5    Yoshimura, Y.6    Teruya, J.7    Shimizu, N.8
  • 13
    • 0021779484 scopus 로고
    • Plasma fibrinolysis after intraduodenal administration of urokinase in rats
    • Sumi, H., Seiki, M., Morimoto, N., Tsushima, H., Maruyama, M., and Mihara, H.: Plasma fibrinolysis after intraduodenal administration of urokinase in rats. Enzyme, 33, 121-127 (1985).
    • (1985) Enzyme , vol.33 , pp. 121-127
    • Sumi, H.1    Seiki, M.2    Morimoto, N.3    Tsushima, H.4    Maruyama, M.5    Mihara, H.6
  • 14
    • 0021910435 scopus 로고
    • Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins
    • Toki, N., Sumi, H., Sasaki, K., Boreisha, I., and Robbins, K. C.: Transport of urokinase across the intestinal tract of normal human subjects with stimulation of synthesis and/or release of urokinase-type proteins. J. Clin. Invest., 75, 1212-1222 (1985).
    • (1985) J. Clin. Invest. , vol.75 , pp. 1212-1222
    • Toki, N.1    Sumi, H.2    Sasaki, K.3    Boreisha, I.4    Robbins, K.C.5
  • 16
    • 0023656415 scopus 로고
    • A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese natto: A typical and popular soybean food in the Japanese diet
    • Sumi, H., Hamada, H., Tsushima, H., Mihara, H., and Muraki, H.: A novel fibrinolytic enzyme (nattokinase) in the vegetable cheese natto: a typical and popular soybean food in the Japanese diet. Experientia, 43, 1110-1111 (1987).
    • (1987) Experientia , vol.43 , pp. 1110-1111
    • Sumi, H.1    Hamada, H.2    Tsushima, H.3    Mihara, H.4    Muraki, H.5
  • 17
    • 0027661249 scopus 로고
    • Potent fibrinolytic enzyme from the lysate of Katsuwonus pelamis digestive tract (Shiokara): Purification and characterization
    • Nakajima, N., Taya, N., and Sumi, H.: Potent fibrinolytic enzyme from the lysate of Katsuwonus pelamis digestive tract (Shiokara): purification and characterization. Biosci. Biotech. Biochem., 57, 1604-1605 (1993).
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1604-1605
    • Nakajima, N.1    Taya, N.2    Sumi, H.3
  • 18
    • 0029960565 scopus 로고    scopus 로고
    • Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang
    • Kim, W. K., Choi, K. H., Kim, Y. T., Park, H. H., Choi, J. Y., Lee, Y. S., Oh, H. I., Kwon, I. B., and Lee, S. Y.: Purification and characterization of a fibrinolytic enzyme produced from Bacillus sp. strain CK 11-4 screened from Chungkook-Jang. Appl. Environ. Microbiol., 62, 2482-2488 (1996).
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2482-2488
    • Kim, W.K.1    Choi, K.H.2    Kim, Y.T.3    Park, H.H.4    Choi, J.Y.5    Lee, Y.S.6    Oh, H.I.7    Kwon, I.B.8    Lee, S.Y.9
  • 19
    • 50449151040 scopus 로고
    • The fibrin plate method for estimating fibrinolytic activity
    • Astrup, T. and Müllertz, S.: The fibrin plate method for estimating fibrinolytic activity. Arch. Biochem. Biophys., 40, 346-351 (1952).
    • (1952) Arch. Biochem. Biophys. , vol.40 , pp. 346-351
    • Astrup, T.1    Müllertz, S.2
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248-254 (1976).
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0026950259 scopus 로고
    • Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (Natto)
    • Nakamura, T., Yamagata, Y., and Ichishima, E.: Nucleotide sequence of the subtilisin NAT gene, aprN, of Bacillus subtilis (Natto). Biosci. Biotech. Biochem., 56, 1869-1871 (1992).
    • (1992) Biosci. Biotech. Biochem. , vol.56 , pp. 1869-1871
    • Nakamura, T.1    Yamagata, Y.2    Ichishima, E.3
  • 24
    • 0025134853 scopus 로고
    • Enhancement of the fibrinolytic activity in plasma by oral administration of NK
    • Sumi, H., Hamada, H., Nakanishi, K., and Hiratani, H.: Enhancement of the fibrinolytic activity in plasma by oral administration of NK. Acta Haematol., 84, 139-143 (1990).
    • (1990) Acta Haematol. , vol.84 , pp. 139-143
    • Sumi, H.1    Hamada, H.2    Nakanishi, K.3    Hiratani, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.