메뉴 건너뛰기




Volumn 118, Issue 3, 1997, Pages 623-631

Purification and characterization of an SDS-activated fibrinolytic enzyme from Eisenia fetida

Author keywords

Eisenia fetida; Fibrinolytic enzyme; Plasminogen; SDS activation

Indexed keywords

APROTININ; BENZYLSULFONYL FLUORIDE; CHYMOSTATIN; DITHIOTHREITOL; DODECYL SULFATE SODIUM; FIBRINOLYTIC AGENT; LEUPEPTIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; PEPSTATIN; PLASMIN; PLASMINOGEN;

EID: 0031428588     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0305-0491(97)00223-X     Document Type: Article
Times cited : (33)

References (29)
  • 2
    • 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
  • 3
    • 13144279517 scopus 로고
    • Deado Pharmaceutical Co. Ltd.
    • Daedo. YONGSHIM Capsule [Pamphlet]. Deado Pharmaceutical Co. Ltd.; 1990:1-2.
    • (1990) YONGSHIM Capsule [Pamphlet] , pp. 1-2
  • 4
    • 0021798139 scopus 로고
    • Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulfate
    • Dahlmann, B.; Rutschmann, M.; Kuehn, L.; Reinauer, H. Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulfate. Biochem. J. 228: 171-177;1985.
    • (1985) Biochem. J. , vol.228 , pp. 171-177
    • Dahlmann, B.1    Rutschmann, M.2    Kuehn, L.3    Reinauer, H.4
  • 5
    • 0016638377 scopus 로고
    • Improved fibrin plate method for fibrinolytic activity measurements: Use of bentonite precipitation and agar solidification
    • Deogny, L.; Weidenbach, A.; Hampton, J.W. Improved fibrin plate method for fibrinolytic activity measurements: Use of bentonite precipitation and agar solidification. Clin. Chim. Acta. 60:85-89;1975.
    • (1975) Clin. Chim. Acta , vol.60 , pp. 85-89
    • Deogny, L.1    Weidenbach, A.2    Hampton, J.W.3
  • 6
    • 0027327041 scopus 로고
    • The multicatalytic proteinase complex (proteasome): Structure and conformational changes associated with changes in proteolytic activity
    • Djaballah, H.; Rowe, A.J.; Harding, S.E.; Rivett, A.J. The multicatalytic proteinase complex (proteasome): Structure and conformational changes associated with changes in proteolytic activity. Biochem. J. 292:857-862;1993.
    • (1993) Biochem. J. , vol.292 , pp. 857-862
    • Djaballah, H.1    Rowe, A.J.2    Harding, S.E.3    Rivett, A.J.4
  • 7
    • 0040892128 scopus 로고
    • Isolation and characterization of five serine proteases with trypsin-, chymotrypsin- and elastase-like characteristics from the gut of the lugworm Arenicola marina (L. Polychaeta)
    • Eberhardt, J. Isolation and characterization of five serine proteases with trypsin-, chymotrypsin- and elastase-like characteristics from the gut of the lugworm Arenicola marina (L. Polychaeta). J. Comp. Physiol. 162B:159-167;1992.
    • (1992) J. Comp. Physiol. , vol.162 B , pp. 159-167
    • Eberhardt, J.1
  • 8
    • 0028949613 scopus 로고
    • The multicatalytic proteinase (Proteasome) of the Hawkmoth, Manduca sexta: Catalytic properties and immunological comparison with the Lobster enzyme complex
    • Haire, M.F.; Clark, J.J.; Jones, M.E.E.; Hendil, K.B.; Schwartz, L.M.; Mykles, D.L. The multicatalytic proteinase (Proteasome) of the Hawkmoth, Manduca sexta: Catalytic properties and immunological comparison with the Lobster enzyme complex. Arch. Biochem. Biophys. 318:15-24;1995.
    • (1995) Arch. Biochem. Biophys. , vol.318 , pp. 15-24
    • Haire, M.F.1    Clark, J.J.2    Jones, M.E.E.3    Hendil, K.B.4    Schwartz, L.M.5    Mykles, D.L.6
  • 9
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A.; Ciechanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61:761-807;1992.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 11
    • 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
  • 12
    • 45549111366 scopus 로고
    • Protein analysis of earthworm coelomic fluid - IV. Evidence, activity induction and purification of Eisenia fetida andrei lysozyme (annelidae)
    • Lassalle, F.; Lassegues, M.; Roch, Ph. Protein analysis of earthworm coelomic fluid - IV. Evidence, activity induction and purification of Eisenia fetida andrei lysozyme (annelidae). Comp. Biochem. Physiol. 91B:187-192;1988.
    • (1988) Comp. Biochem. Physiol. , vol.91 B , pp. 187-192
    • Lassalle, F.1    Lassegues, M.2    Roch, Ph.3
  • 13
    • 0024497831 scopus 로고
    • Antibacterial activity of Eisenia fetida andrei coelomic fluid: Evidence, induction, and animal protection
    • Lassegues, M.; Roch, Ph.; Valembois, P. Antibacterial activity of Eisenia fetida andrei coelomic fluid: Evidence, induction, and animal protection. J. Invertebr. Pathol. 53:1-6;1989.
    • (1989) J. Invertebr. Pathol. , vol.53 , pp. 1-6
    • Lassegues, M.1    Roch, Ph.2    Valembois, P.3
  • 15
    • 0031552065 scopus 로고    scopus 로고
    • Purification, characterization and activities of two hemolytic and antibacterial proteins from coelomic fluid of the annelid Eisenia fetida andrei
    • Milochau, A.; Lassegues, M.; Valembois, P. Purification, characterization and activities of two hemolytic and antibacterial proteins from coelomic fluid of the annelid Eisenia fetida andrei. Biochim. Biophys. Acta. 1337:123-132;1997.
    • (1997) Biochim. Biophys. Acta , vol.1337 , pp. 123-132
    • Milochau, A.1    Lassegues, M.2    Valembois, P.3
  • 16
    • 0027675482 scopus 로고
    • Characterization of potent fibrinolytic enzymes in earthworm, Lumbricus rubellus
    • Nakajima, N.; Mihara, H.; Sumi, H. Characterization of potent fibrinolytic enzymes in earthworm, Lumbricus rubellus. Biosci. Biotech. Biochem. 57:1726-1730;1993.
    • (1993) Biosci. Biotech. Biochem. , vol.57 , pp. 1726-1730
    • Nakajima, N.1    Mihara, H.2    Sumi, H.3
  • 17
    • 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.; Hamada, H. Chemical modification of earthworm fibrinolytic enzyme with human serum albumin fragment and characterization of the protease as a therapeutic enzyme. Biosci. Biotech. Biochem. 60:293-300;1996.
    • (1996) Biosci. Biotech. Biochem. , vol.60 , pp. 293-300
    • Nakajima, N.1    Ishihara, K.2    Sugimoto, M.3    Sumi, H.4    Mikuni, K.5    Hamada, H.6
  • 18
    • 0027410433 scopus 로고
    • Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids
    • Orlowski, M.; Cardozo, C.; Michaud, C. Evidence for the presence of five distinct proteolytic components in the pituitary multicatalytic proteinase complex. Properties of two components cleaving bonds on the carboxyl side of branched chain and small neutral amino acids. Biochemistry 32:1563-1572; 1993.
    • (1993) Biochemistry , vol.32 , pp. 1563-1572
    • Orlowski, M.1    Cardozo, C.2    Michaud, C.3
  • 19
    • 0021105304 scopus 로고
    • Purification and characterization of proteases from the polychaete annelid Sabellaria alveolata (L.)
    • Peaucellier, G. Purification and characterization of proteases from the polychaete annelid Sabellaria alveolata (L.). Eur. J. Biochem. 136:435-445;1983.
    • (1983) Eur. J. Biochem. , vol.136 , pp. 435-445
    • Peaucellier, G.1
  • 21
    • 0018563587 scopus 로고
    • Protein analysis of earthworm coelomic fluid: I-Polymorphic system of the natural hemolysin of Eisenia fetida andrei
    • Roch, Ph. Protein analysis of earthworm coelomic fluid: I-Polymorphic system of the natural hemolysin of Eisenia fetida andrei. Devel. Comp. Immun. 3:599-608;1979.
    • (1979) Devel. Comp. Immun. , vol.3 , pp. 599-608
    • Roch, Ph.1
  • 22
    • 0000006406 scopus 로고
    • Protein analysis of earthworm coelomic fluid - II. Isolation and biochemical characterization of the Eisenia fetida andrei factor (EFAF)
    • Roch, Ph.; Valembois, P.; Davant, N.; Lassegues, M. Protein analysis of earthworm coelomic fluid - II. Isolation and biochemical characterization of the Eisenia fetida andrei factor (EFAF). Comp. Biochem. Physiol. 69B:829-836;1981.
    • (1981) Comp. Biochem. Physiol. , vol.69 B , pp. 829-836
    • Roch, Ph.1    Valembois, P.2    Davant, N.3    Lassegues, M.4
  • 23
    • 0026035919 scopus 로고
    • Purification of three serine proteases from the coelomic cells of earthworms (Eisenia fetida)
    • Roch, Ph.; Stabili, L.; Pagliara, P. Purification of three serine proteases from the coelomic cells of earthworms (Eisenia fetida). Comp. Biochem. Physiol. 98B:597-602;1991.
    • (1991) Comp. Biochem. Physiol. , vol.98 B , pp. 597-602
    • Roch, Ph.1    Stabili, L.2    Pagliara, P.3
  • 25
    • 0029795495 scopus 로고    scopus 로고
    • A novel protein, lysenin, that causes contraction of the isolated rat aorta: Its purification from the coelomic fluid of the earthworm, Eisenia foetida
    • Sekizawa, Y.; Kenichi, H.; Nakajima, T.; Kobayashi, H. A novel protein, lysenin, that causes contraction of the isolated rat aorta: its purification from the coelomic fluid of the earthworm, Eisenia foetida. Biomed. Res. 17:197-203;1996.
    • (1996) Biomed. Res. , vol.17 , pp. 197-203
    • Sekizawa, Y.1    Kenichi, H.2    Nakajima, T.3    Kobayashi, H.4
  • 26
    • 0027379034 scopus 로고
    • A very stable and potent fibrinolytic enzyme found in earthworm Lumbricus rubellus autolysate
    • Sumi, H.; Nakajima, N.; Mihara, H. A very stable and potent fibrinolytic enzyme found in earthworm Lumbricus rubellus autolysate. Comp. Biochem. Physiol. 106B:763-766;1993.
    • (1993) Comp. Biochem. Physiol. , vol.106 B , pp. 763-766
    • Sumi, H.1    Nakajima, N.2    Mihara, H.3
  • 27
    • 0023009780 scopus 로고
    • A high molecular weight protease in the cytosol of rat liver
    • Tanaka, K.; Ii, K.; Ichihara, A.; Waxman, L.; Goldberg, A.L. A high molecular weight protease in the cytosol of rat liver. J. Biol. Chem. 261:15197-15203;1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15197-15203
    • Tanaka, K.1    Ii, K.2    Ichihara, A.3    Waxman, L.4    Goldberg, A.L.5
  • 28
    • 43949159445 scopus 로고
    • Purification and characterization of a polyL-lysine-activated serine endoprotease from Lumbricus rubellus
    • Woo, K.M.; Yi, W.; Sohn, Y.J.; Chang, C.S.; Kang M.S.; Ha, D.B.; Chung, C.H. Purification and characterization of a polyL-lysine-activated serine endoprotease from Lumbricus rubellus. Comp. Biochem. Physiol. 109B:71-80;1994.
    • (1994) Comp. Biochem. Physiol. , vol.109 B , pp. 71-80
    • Woo, K.M.1    Yi, W.2    Sohn, Y.J.3    Chang, C.S.4    Kang, M.S.5    Ha, D.B.6    Chung, C.H.7
  • 29
    • 0029071580 scopus 로고
    • Reaction of 20S proteasome: Shift of SDS-dependent activation profile by divalent cations
    • Yamada, S.; Hojo, K.; Yoshimura, H.; Ishikawa, K. Reaction of 20S proteasome: Shift of SDS-dependent activation profile by divalent cations. J. Biochem. 117:1162-1169;1995.
    • (1995) J. Biochem. , vol.117 , pp. 1162-1169
    • Yamada, S.1    Hojo, K.2    Yoshimura, H.3    Ishikawa, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.