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Volumn 114, Issue 1, 1996, Pages 1-9

Purification and characterization of a 58,000-Da proteinase inhibitor from the hemolymph of a solitary ascidian, Halocynthia roretzi

Author keywords

ascidian; dextran sulfate; Ether Toyopearl; Halocynthia roretzi; hemolymph; Heparin Sepharose; plasma enzyme; proteinase inhibitor

Indexed keywords

PROTEINASE INHIBITOR;

EID: 0030057879     PISSN: 03050491     EISSN: None     Source Type: Journal    
DOI: 10.1016/0305-0491(95)02110-8     Document Type: Article
Times cited : (8)

References (45)
  • 2
    • 0003089706 scopus 로고
    • Platelet function
    • Williams, W.J.; Beutler, E.; Erslev, A.J.; Lichtman, M.A., eds. New York: McGraw-Hill Publishing Co.
    • Bennett, J.S.; Shattil, S.J. Platelet function. In: Williams, W.J.; Beutler, E.; Erslev, A.J.; Lichtman, M.A., eds. Hematology, 4th ed. New York: McGraw-Hill Publishing Co.; 1990: 1233-1250.
    • (1990) Hematology, 4th Ed. , pp. 1233-1250
    • Bennett, J.S.1    Shattil, S.J.2
  • 3
    • 15844432022 scopus 로고
    • Biochemistry of plasma coagulation factors
    • Williams, W.J.; Beutler, E.; Erslev, A.J.; Lichtman, M.A., eds. New York: McGraw-Hill Publishing Co.
    • Nemerson, Y.; Williams, W.J. Biochemistry of plasma coagulation factors. In: Williams, W.J.; Beutler, E.; Erslev, A.J.; Lichtman, M.A., eds. Hematology, 4th ed. New York: McGraw-Hill Publishing Co.; 1990:1267-1284.
    • (1990) Hematology, 4th Ed. , pp. 1267-1284
    • Nemerson, Y.1    Williams, W.J.2
  • 4
    • 0342579277 scopus 로고
    • Studies on the naturally occurring hemagglutinin in the coelomic fluid of an ascidian
    • Fuke, T. M.; Sugai, T. Studies on the naturally occurring hemagglutinin in the coelomic fluid of an ascidian. Biol. Bull. 143: 140-149; 1972.
    • (1972) Biol. Bull. , vol.143 , pp. 140-149
    • Fuke, T.M.1    Sugai, T.2
  • 5
    • 0020493888 scopus 로고
    • Galactose-specific lectin in the hemolymph of solitary ascidian, Halocynthia roretzi: Isolation and characterization
    • Yokosawa, H.; Sawada, H.; Abe, Y.; Numakunai, T.; Ishii, S. Galactose-specific lectin in the hemolymph of solitary ascidian, Halocynthia roretzi: isolation and characterization. Biochem. Biophys. Res. Commun. 107:451-457;1982.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 451-457
    • Yokosawa, H.1    Sawada, H.2    Abe, Y.3    Numakunai, T.4    Ishii, S.5
  • 6
    • 0000339726 scopus 로고
    • N-acetyl-galactosamine-specinc lectin, a novel lectin in the haemolymph of the ascidian Halocynthia roretzi: Isolation, characterization and comparison with galactose-specific lectin
    • Harada-Azumi, K.; Yokosawa, H.; Ishii, S. N-acetyl-galactosamine-specinc lectin, a novel lectin in the haemolymph of the ascidian Halocynthia roretzi: isolation, characterization and comparison with galactose-specific lectin. Comp. Biochem. Physiol. 88B:375-381;1987.
    • (1987) Comp. Biochem. Physiol. , vol.88 B , pp. 375-381
    • Harada-Azumi, K.1    Yokosawa, H.2    Ishii, S.3
  • 7
    • 0025996005 scopus 로고
    • A novel lipopoly-saccharide-binding hemagglutinin isolated from hemocytes of the solitary ascidian, Halocynthia roretzi: It can agglutinate bacteria
    • Azumi, K.; Ozeki, S.; Yokosawa, H.; Ishii, S. A novel lipopoly-saccharide-binding hemagglutinin isolated from hemocytes of the solitary ascidian, Halocynthia roretzi: it can agglutinate bacteria. Dev. Comp. Immunol. 15:9-16;1991.
    • (1991) Dev. Comp. Immunol. , vol.15 , pp. 9-16
    • Azumi, K.1    Ozeki, S.2    Yokosawa, H.3    Ishii, S.4
  • 8
    • 0015888544 scopus 로고
    • Allogeneic inhibition in a compound ascidian, Botryllus primigenus Oka. I. Processes and features of "nonfusion" reaction
    • Tanaka, K.; Watanabe, H. Allogeneic inhibition in a compound ascidian, Botryllus primigenus Oka. I. Processes and features of "nonfusion" reaction. Cell. Immunol. 7:410-426;1973.
    • (1973) Cell. Immunol. , vol.7 , pp. 410-426
    • Tanaka, K.1    Watanabe, H.2
  • 9
    • 0015830879 scopus 로고
    • Allogeneic inhibition in a compound ascidian, Botryllus primigenus Oka. II. Cellular and humoral responses in "nonfusion" reaction
    • Tanaka, K. Allogeneic inhibition in a compound ascidian, Botryllus primigenus Oka. II. Cellular and humoral responses in "nonfusion" reaction. Cell Immunol. 7:427-443;1973.
    • (1973) Cell Immunol. , vol.7 , pp. 427-443
    • Tanaka, K.1
  • 10
    • 0000915398 scopus 로고
    • Pattern of cellular alloreactivity of the solitary ascidian, Halocynthia roretzi, in relation to genetic control
    • Fuke, T.M.; Nakamura, I. Pattern of cellular alloreactivity of the solitary ascidian, Halocynthia roretzi, in relation to genetic control. Biol. Bull. 169:631-637;1985.
    • (1985) Biol. Bull. , vol.169 , pp. 631-637
    • Fuke, T.M.1    Nakamura, I.2
  • 11
    • 0000916883 scopus 로고
    • "Contact reactions" between xenogeneic or allogeneic coelomic cells of solitary ascidians
    • Fuke, T. M. "Contact reactions" between xenogeneic or allogeneic coelomic cells of solitary ascidians. Biol. Bull. 158:304-315;1980.
    • (1980) Biol. Bull. , vol.158 , pp. 304-315
    • Fuke, T.M.1
  • 12
    • 0028455214 scopus 로고
    • Hemocyte aggregation in the solitary ascidian Halocynthia roretzi: Plasma factors, magnesium ion, and Met-Lys-bradykinin induce the aggregation
    • Takahashi, H.; Azumi, K.; Yokosawa, H. Hemocyte aggregation in the solitary ascidian Halocynthia roretzi: plasma factors, magnesium ion, and Met-Lys-bradykinin induce the aggregation. Biol. Bull. 186:247-253;1994.
    • (1994) Biol. Bull. , vol.186 , pp. 247-253
    • Takahashi, H.1    Azumi, K.2    Yokosawa, H.3
  • 13
    • 0000983376 scopus 로고
    • Classification and characterization of ten hemocyte types in the tunicate Halocynthia roretzi
    • Sawada, T.; Fujikura, Y.; Tomonaga, S.; Fukumoto, T. Classification and characterization of ten hemocyte types in the tunicate Halocynthia roretzi. Zool. Sci. 8:939-950;1991.
    • (1991) Zool. Sci. , vol.8 , pp. 939-950
    • Sawada, T.1    Fujikura, Y.2    Tomonaga, S.3    Fukumoto, T.4
  • 14
    • 0028317392 scopus 로고
    • The phagocytes in hemolymph of Halocynthia roretzi and their phagocytic activity
    • Ohtake, S-I.; Abe, T.; Shishikura, F.; Tanaka, K. The phagocytes in hemolymph of Halocynthia roretzi and their phagocytic activity. Zool. Sci. 11:681-691;1994.
    • (1994) Zool. Sci. , vol.11 , pp. 681-691
    • Ohtake, S.-I.1    Abe, T.2    Shishikura, F.3    Tanaka, K.4
  • 15
    • 0022070938 scopus 로고
    • Trypsin inhibitor in the hemolymph of a solitary ascidian, Halocynthia roretzi. Purification and characterization
    • Yokosawa, H.; Odajima, R.; Ishii, S. Trypsin inhibitor in the hemolymph of a solitary ascidian, Halocynthia roretzi. Purification and characterization. J. Biochem. 97:1621-1630;1985.
    • (1985) J. Biochem. , vol.97 , pp. 1621-1630
    • Yokosawa, H.1    Odajima, R.2    Ishii, S.3
  • 16
    • 0025097969 scopus 로고
    • Halocyamines: Novel antimicrobial tetrapeptide-like substances isolated from the hemocytes of the solitary ascidian Halocynthia roretzi
    • Azumi, K.; Yokosawa, H.; Ishii, S. Halocyamines: novel antimicrobial tetrapeptide-like substances isolated from the hemocytes of the solitary ascidian Halocynthia roretzi. Biochemistry 29:159-165;1990.
    • (1990) Biochemistry , vol.29 , pp. 159-165
    • Azumi, K.1    Yokosawa, H.2    Ishii, S.3
  • 17
    • 0028915483 scopus 로고
    • Hemocytes release phenoloxidase upon contact reaction, an allogeneic interaction, in the ascidian Halocynthia roretzi
    • Akita, N.; Hoshi, M. Hemocytes release phenoloxidase upon contact reaction, an allogeneic interaction, in the ascidian Halocynthia roretzi. Cell Struct. Func. 20:81-87;1995.
    • (1995) Cell Struct. Func. , vol.20 , pp. 81-87
    • Akita, N.1    Hoshi, M.2
  • 18
    • 0000334355 scopus 로고
    • Urochordates
    • Ratcliffe, N.A.; Rowley, A.F., eds. London: Academic Press
    • Wright, R.K. Urochordates. In: Ratcliffe, N.A.; Rowley, A.F., eds. Invertebrate blood cells. London: Academic Press; 1981: 565-626.
    • (1981) Invertebrate Blood Cells , pp. 565-626
    • Wright, R.K.1
  • 19
    • 15844373567 scopus 로고
    • Human blood coagulation and the haemostatic mechanism
    • Biggs, R. Human blood coagulation and the haemostatic mechanism. Symp. Zool. Sci. Lond. 27:7-18;1970.
    • (1970) Symp. Zool. Sci. Lond. , vol.27 , pp. 7-18
    • Biggs, R.1
  • 20
    • 0037736693 scopus 로고
    • Studies on the antithrombin and heparin cofactor activities of a fraction adsorbed from plasma by aluminum hydroxide
    • Monkhouse, F.C.; France, E.S.; Seegers, W.H. Studies on the antithrombin and heparin cofactor activities of a fraction adsorbed from plasma by aluminum hydroxide. Circ. Res. 3:397-402;1955.
    • (1955) Circ. Res. , vol.3 , pp. 397-402
    • Monkhouse, F.C.1    France, E.S.2    Seegers, W.H.3
  • 21
    • 0019362162 scopus 로고
    • Detection of a new heparin-dependent inhibitor of thrombin in human plasma
    • Tollefsen, D.M.; Blank, M.K. Detection of a new heparin-dependent inhibitor of thrombin in human plasma. J. Clin. Invest. 68:589-596;1981.
    • (1981) J. Clin. Invest. , vol.68 , pp. 589-596
    • Tollefsen, D.M.1    Blank, M.K.2
  • 22
    • 0021339489 scopus 로고
    • Mechanism of inhibition of activated protein C by protein C inhibitor
    • Suzuki, K.; Nishioka, J.; Kusumoto, H.; Hashimoto, S. Mechanism of inhibition of activated protein C by protein C inhibitor. J. Biochem. 95:187-195;1984.
    • (1984) J. Biochem. , vol.95 , pp. 187-195
    • Suzuki, K.1    Nishioka, J.2    Kusumoto, H.3    Hashimoto, S.4
  • 24
    • 0027509462 scopus 로고
    • Glycosaminoglycans and the regulation of blood coagulation
    • Bourin, M.-C.; Lindahl, U. Glycosaminoglycans and the regulation of blood coagulation. Biochem. J. 289:313-330;1993.
    • (1993) Biochem. J. , vol.289 , pp. 313-330
    • Bourin, M.-C.1    Lindahl, U.2
  • 26
    • 0020643467 scopus 로고
    • Human plasma proteinase inhibitors
    • Travis, J.; Salvesen, G.S. Human plasma proteinase inhibitors. Annu. Rev. Biochem. 52:655-709;1983.
    • (1983) Annu. Rev. Biochem. , vol.52 , pp. 655-709
    • Travis, J.1    Salvesen, G.S.2
  • 27
    • 0017373087 scopus 로고
    • A sensitive substrate for the clotting enzyme in horseshoe crab hemocytes
    • Nakamura, S.; Morita, T.; Iwanaga, S.; Niwa, M.; Takahashi, K. A sensitive substrate for the clotting enzyme in horseshoe crab hemocytes. J. Biochem. 81:1567-1569;1977.
    • (1977) J. Biochem. , vol.81 , pp. 1567-1569
    • Nakamura, S.1    Morita, T.2    Iwanaga, S.3    Niwa, M.4    Takahashi, K.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophase T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophase T4. Nature 227:680-685;1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0014939933 scopus 로고
    • The Chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine
    • Friedman, M.; Krull, L.H.; Cavins, J.F. The Chromatographic determination of cystine and cysteine residues in proteins as S-β-(4-pyridylethyl)cysteine. J. Biol. Chem. 245:3868-3871; 1970.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3868-3871
    • Friedman, M.1    Krull, L.H.2    Cavins, J.F.3
  • 30
    • 0001828191 scopus 로고
    • Immunizations
    • Harlow, E.; Lane, D., eds. New York: Cold Spring Harbor Laboratory
    • Harlow, E.; Lane, D. Immunizations. In: Harlow, E.; Lane, D., eds. Antibodies. A laboratory manual. New York: Cold Spring Harbor Laboratory; 1988:53-137.
    • (1988) Antibodies. A Laboratory Manual , pp. 53-137
    • Harlow, E.1    Lane, D.2
  • 31
    • 84981776413 scopus 로고
    • Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion
    • Ouchterlony Ö. Antigen-antibody reactions in gels. IV. Types of reactions in coordinated systems of diffusion. Acta Pathol. Microbiol. Scand. 32:231-240;1953.
    • (1953) Acta Pathol. Microbiol. Scand. , vol.32 , pp. 231-240
    • Ouchterlony, Ö.1
  • 32
    • 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
  • 33
    • 0019472086 scopus 로고
    • A simple two-step procedure for the isolation of antithrombin III from biological fluids
    • McKay, E.J. A simple two-step procedure for the isolation of antithrombin III from biological fluids. Thromb. Res. 21:375-382;1981.
    • (1981) Thromb. Res. , vol.21 , pp. 375-382
    • McKay, E.J.1
  • 34
    • 0027449971 scopus 로고
    • Isolation of plasma proteins from the clotting cascade by heparin affinity chromatography
    • Josíc, D.; Bal, F.; Schwinn, H. Isolation of plasma proteins from the clotting cascade by heparin affinity chromatography. J. Chromatogr. 632:1-10;1993.
    • (1993) J. Chromatogr. , vol.632 , pp. 1-10
    • Josíc, D.1    Bal, F.2    Schwinn, H.3
  • 35
    • 0017033402 scopus 로고
    • Human coagulation factor IX. Isolation and characterization
    • Suomela, H. Human coagulation factor IX. Isolation and characterization. Eur. J. Biochem. 71:145-154;1976.
    • (1976) Eur. J. Biochem. , vol.71 , pp. 145-154
    • Suomela, H.1
  • 36
    • 0017589845 scopus 로고
    • Chromatography of human prothrombin complex on dextran sulfate agarose
    • Pepper, D.S.; Prowse, C. Chromatography of human prothrombin complex on dextran sulfate agarose. Thromb. Res. 11:687-692;1977.
    • (1977) Thromb. Res. , vol.11 , pp. 687-692
    • Pepper, D.S.1    Prowse, C.2
  • 37
    • 0016299396 scopus 로고
    • Purification of antithrombin III by affinity chromatography
    • Miller-Andersson, M.; Borg, H.; Andersson, L.-O. Purification of antithrombin III by affinity chromatography. Thromb. Res. 5:439-452;1974.
    • (1974) Thromb. Res. , vol.5 , pp. 439-452
    • Miller-Andersson, M.1    Borg, H.2    Andersson, L.-O.3
  • 38
    • 0025277922 scopus 로고
    • Primary structure of ascidian trypsin inhibitors in the hemolymph of a solitary ascidian, Halocynthia roretzi
    • Kumazaki, T.; Hoshiba, N.; Yokosawa, H.; Ishii, S. Primary structure of ascidian trypsin inhibitors in the hemolymph of a solitary ascidian, Halocynthia roretzi. J. Biochem. 107:409-413; 1990.
    • (1990) J. Biochem. , vol.107 , pp. 409-413
    • Kumazaki, T.1    Hoshiba, N.2    Yokosawa, H.3    Ishii, S.4
  • 39
    • 0020020249 scopus 로고
    • Properties of protease inhibitors from the haemolymph of silkworms, Bombyx mori, Antheraea pemyi and Philosamia cynthia ricini
    • Eguchi, M.; Haneda, I.; Iwamoto, A. Properties of protease inhibitors from the haemolymph of silkworms, Bombyx mori, Antheraea pemyi and Philosamia cynthia ricini. Comp. Biochem. Physiol. 71B:569-576;1982.
    • (1982) Comp. Biochem. Physiol. , vol.71 B , pp. 569-576
    • Eguchi, M.1    Haneda, I.2    Iwamoto, A.3
  • 40
    • 0021405056 scopus 로고
    • Isolation of two novel proteinase inhibitors from hemolymph of silkworm larva, Bombyx mori. Comparison with human serum proteinase inhibitors
    • Sasaki, T.; Kobayashi, K. Isolation of two novel proteinase inhibitors from hemolymph of silkworm larva, Bombyx mori. Comparison with human serum proteinase inhibitors. J. Biochem. 95:1009-1017;1984.
    • (1984) J. Biochem. , vol.95 , pp. 1009-1017
    • Sasaki, T.1    Kobayashi, K.2
  • 41
    • 0022432076 scopus 로고
    • Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae
    • Suzuki, T.; Natori, S. Purification and characterization of an inhibitor of the cysteine protease from the hemolymph of Sarcophaga peregrina larvae. J. Biol. Chem. 260:5115-5120;1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5115-5120
    • Suzuki, T.1    Natori, S.2
  • 42
    • 0025746697 scopus 로고
    • Characterization of a naturally occurring protease inhibitor in the hemolymph of the scorpion, Heterometrus bengalensis
    • Banerjee, A.; Datta, P.K.; Basu, P.S.; Datta, T.K. Characterization of a naturally occurring protease inhibitor in the hemolymph of the scorpion, Heterometrus bengalensis. Dev. Comp. Immunol. 15:213-218;1991.
    • (1991) Dev. Comp. Immunol. , vol.15 , pp. 213-218
    • Banerjee, A.1    Datta, P.K.2    Basu, P.S.3    Datta, T.K.4
  • 43
    • 0028118621 scopus 로고
    • A Limulus intracellular coagulation inhibitor with characteristics of the serpin superfamily. Purification, characterization, and cDNA cloning
    • Miura, Y.; Kawabata, S.; Iwanaga, S. A Limulus intracellular coagulation inhibitor with characteristics of the serpin superfamily. Purification, characterization, and cDNA cloning. J. Biol. Chem. 269:542-547;1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 542-547
    • Miura, Y.1    Kawabata, S.2    Iwanaga, S.3
  • 44
    • 0028985590 scopus 로고
    • A Limulus intracellular coagulation inhibitor type 2. Purification, characterization, cDNA cloning, and tissue localization
    • Miura, Y.; Kawabata, S.; Wakamiya, Y.; Nakamura, T.; Iwanaga, S. A Limulus intracellular coagulation inhibitor type 2. Purification, characterization, cDNA cloning, and tissue localization. J. Biol. Chem. 270:558-565;1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 558-565
    • Miura, Y.1    Kawabata, S.2    Wakamiya, Y.3    Nakamura, T.4    Iwanaga, S.5
  • 45
    • 84951413544 scopus 로고
    • The oxidation of ribonuclease with performic acid
    • Hirs, C.H.W. The oxidation of ribonuclease with performic acid. J. Biol. Chem. 219:611-621;1956.
    • (1956) J. Biol. Chem. , vol.219 , pp. 611-621
    • Hirs, C.H.W.1


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