메뉴 건너뛰기




Volumn 63, Issue 11, 1999, Pages 2031-2033

Further Characterization of Earthworm Serine Proteases: Cleavage Specificity Against Peptide Substrates and on Autolysis

Author keywords

Cleavage specificity; Earthworm; Fibrinolytic enzyme; Serine protease; amyloid

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; CHYMOTRYPSIN; INSULIN; PEPTIDE FRAGMENT; SERINE PROTEINASE; TRYPSIN;

EID: 0033217531     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.63.2031     Document Type: Article
Times cited : (33)

References (16)
  • 1
    • 0042165761 scopus 로고
    • Activating the body’s blood clot dissolvers: Biotech’s new role
    • Klausner, A., Activating the body’s blood clot dissolvers: biotech’s new role. Bio/technology, 1, 330-376 (1983).
    • (1983) Bio/Technology , vol.1 , pp. 330-376
    • Klausner, A.1
  • 2
    • 0021175033 scopus 로고
    • Biological and thrombolytic properties of proenzyme and active forms of human urokinase-II. Turnover of natural and recombinant urokinase in rabbits and squirrel monkeys
    • D. Collen, D. Cook, F. De., and Lijnen, H. R., Biological and thrombolytic properties of proenzyme and active forms of human urokinase-II. Turnover of natural and recombinant urokinase in rabbits and squirrel monkeys. Thromb. Haemostas, 52, 24-26 (1984).
    • (1984) Thromb. Haemostas , vol.52 , pp. 24-26
    • Collen, D.1    Cook, D.2    De, F.3    Lijnen, H.R.4
  • 3
    • 0018194158 scopus 로고
    • Immunogenicity and antigenicity of soluble cress-linked enzyme/albumin polymers: Advantages for enzyme therapy
    • Remy, M. H. and Poznansky, M. J., Immunogenicity and antigenicity of soluble cress-linked enzyme/albumin polymers: Advantages for enzyme therapy. Lancet, 2, 68-70 (1978).
    • (1978) Lancet , vol.2 , pp. 68-70
    • Remy, M.H.1    Poznansky, M.J.2
  • 4
    • 0000160830 scopus 로고
    • Chemical modification of urokinase with human serum albumin fragments
    • Yokoigawa, K., Tanizawa, K., and Soda, K., Chemical modification of urokinase with human serum albumin fragments. Agric Biol Chem., 53, 2887-2893 (1991).
    • (1991) Agric Biol Chem. , vol.53 , pp. 2887-2893
    • Yokoigawa, K.1    Tanizawa, K.2    Soda, K.3
  • 5
    • 0041664816 scopus 로고
    • Studies of antipyretic components in the Japanese earthworm
    • (in Japanese)
    • Tanaka, B. and Nakata, S., Studies of antipyretic components in the Japanese earthworm. Tokyo Igaku Zasshi, 29, 67-97 (1974) (in Japanese).
    • (1974) Tokyo Igaku Zasshi , vol.29 , pp. 67-97
    • Tanaka, B.1    Nakata, S.2
  • 6
    • 0027675482 scopus 로고
    • Characterization of potent fibrinolytic enzymes in earthworm, Lumbricus rubellus
    • Nakajima, N., Mihara, H., and Sumi, H., Characterization of potent fibrinolytic enzymes in earthworm, Lumbricus rubellus. Biosci. Biotechnol. Biochem., 57, 1726-1730 (1993).
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1726-1730
    • Nakajima, N.1    Mihara, H.2    Sumi, H.3
  • 7
    • 0027379034 scopus 로고
    • A very stable and potent fibrinolytic enzyme found in earthworm Lumbricus rubellus autolysate
    • Sumi, H., Nakajima, N., and Mihara, H., A very stable and potent fibrinolytic enzyme found in earthworm Lumbricus rubellus autolysate. Comp. Biochem. Physiol., 106, 763-766 (1993).
    • (1993) Comp. Biochem. Physiol. , vol.106 , pp. 763-766
    • Sumi, H.1    Nakajima, N.2    Mihara, H.3
  • 8
    • 0030087823 scopus 로고    scopus 로고
    • Chemical modification of earthworm fibrinolytic enzyme with human serum albumin fragment and characterization of the protease as a therapeutic enzyme
    • Nakajima, N., Ishihara, K., Sugimoto, M., Sumi, H., Mikuni, K., and Hamada, H., Chemical modification of earthworm fibrinolytic enzyme with human serum albumin fragment and characterization of the protease as a therapeutic enzyme. Biosci. Biotechnol. Biochem., 60, 293-300 (1996).
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 293-300
    • Nakajima, N.1    Ishihara, K.2    Sugimoto, M.3    Sumi, H.4    Mikuni, K.5    Hamada, H.6
  • 9
    • 0026567936 scopus 로고
    • Amyloidogenesis in Alzheimer’s disease: Some possible therapeutic opportunities
    • Gandy, S. and Greengard, P., Amyloidogenesis in Alzheimer’s disease: some possible therapeutic opportunities. TiPS, 13, 108-113 (1992).
    • (1992) Tips , vol.13 , pp. 108-113
    • Gandy, S.1    Greengard, P.2
  • 10
    • 85004570784 scopus 로고
    • Substrate specificity of alkaline protease from Cephalosporium sp. LM388
    • Tsuchida, K., Seki, K., Arai, T., and Masui, T., Substrate specificity of alkaline protease from Cephalosporium sp. LM388. Biosci. Biotechnol. Biochem., 57, 1803-1804 (1993).
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1803-1804
    • Tsuchida, K.1    Seki, K.2    Arai, T.3    Masui, T.4
  • 11
    • 0029823194 scopus 로고    scopus 로고
    • Purification and biochemical characterization of vacuplar serine endopeptidase induced by glucose starvation in maize roots
    • James, F., Brouquisse, R., Suire, C., Pradet, A., and Raymond, P., Purification and biochemical characterization of vacuplar serine endopeptidase induced by glucose starvation in maize roots. Biochem. J., 320, 283-292 (1996).
    • (1996) Biochem. J. , vol.320 , pp. 283-292
    • James, F.1    Brouquisse, R.2    Suire, C.3    Pradet, A.4    Raymond, P.5
  • 12
    • 0031218819 scopus 로고    scopus 로고
    • Purification and characterization of a cysteine protease from corns of freesia, Freesia reflacta
    • Kaneda, M., Yonezawa, H., and Uchikoba, T., Purification and characterization of a cysteine protease from corns of freesia, Freesia reflacta. Biosci. Biotechnol. Biochem., 61, 1554-1559 (1997).
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1554-1559
    • Kaneda, M.1    Yonezawa, H.2    Uchikoba, T.3
  • 13
    • 0018378014 scopus 로고
    • The digestion of the oxidized B chain of insulin by human neutrophile proteases: Elastase and chymotrypsin-like protease
    • Levy, H. and Feinstein, G., The digestion of the oxidized B chain of insulin by human neutrophile proteases: elastase and chymotrypsin-like protease. Biochim. Biophys. Acta, 567, (1979).
    • (1979) Biochim. Biophys. Acta , pp. 567
    • Levy, H.1    Feinstein, G.2
  • 14
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • by Barrett, A. J., Academic Press
    • Andrew, W. S. and Robert, M., Catalytic mechanism in papain family of cysteine peptidases, in “Methods Enzymol.,” ed. by Barrett, A. J., Academic Press, 244, 486-500 (1994).
    • (1994) Methods Enzymol
    • Andrew, W.S.1    Robert, M.2
  • 15
    • 0024298861 scopus 로고
    • Purification and biological characterization of atroxase, a nonhemorrhagic fibrinolytic protease from Western diamondback rattlesnake venom
    • Willis, T. W. and Tu, A. T., Purification and biological characterization of atroxase, a nonhemorrhagic fibrinolytic protease from Western diamondback rattlesnake venom. Biochemistry, 27, 4767-4777 (1988).
    • (1988) Biochemistry , vol.27 , pp. 4767-4777
    • Willis, T.W.1    Tu, A.T.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriopage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriopage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.