메뉴 건너뛰기




Volumn 20, Issue 10, 1996, Pages 583-598

Isolation and characterization of an anticoagulant from the salivary glands of the tick, Ornithodoros savignyi (Acari: Argasidae)

Author keywords

anticoagulant; factor Xa; inhibitor; Ornithodoros savignyi; Ticks

Indexed keywords

ORNITHODOROS SAVIGNYI;

EID: 0030267778     PISSN: 01688162     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF00052809     Document Type: Article
Times cited : (50)

References (31)
  • 2
    • 0001054571 scopus 로고
    • A simple modification converts the spinning cup sequencer into a vapour phase sequencer
    • Brandt, W.F., Alk, H., Chauhan, M. and Von-Holt, C. 1984. A simple modification converts the spinning cup sequencer into a vapour phase sequencer. FEBS Lett. 14: 228-232.
    • (1984) FEBS Lett. , vol.14 , pp. 228-232
    • Brandt, W.F.1    Alk, H.2    Chauhan, M.3    Von-Holt, C.4
  • 3
    • 0029014045 scopus 로고
    • Ancylostoma canicum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation factor Xa
    • Capello, M., Vlasuk, G.P., Bergum, P.W., Huang, S. and Hotez, P.J. 1995. Ancylostoma canicum anticoagulant peptide: a hookworm-derived inhibitor of human coagulation factor Xa. Proc. Natl Acad. Sci. USA 92: 6152-6156.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6152-6156
    • Capello, M.1    Vlasuk, G.P.2    Bergum, P.W.3    Huang, S.4    Hotez, P.J.5
  • 4
    • 0016700753 scopus 로고
    • Tight-binding inhibitors
    • Cha, S. 1975. Tight-binding inhibitors. Biochem. Pharmacol. 24: 2177-2185.
    • (1975) Biochem. Pharmacol. , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 5
    • 0026733452 scopus 로고
    • An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech
    • Connolly, T.M., Jacobs, J.W. and Condra, C. 1992. An inhibitor of collagen-stimulated platelet activation from the salivary glands of the Haementeria officinalis leech. J. Biol. Chem. 267: 6893-6898.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6893-6898
    • Connolly, T.M.1    Jacobs, J.W.2    Condra, C.3
  • 6
    • 0022760451 scopus 로고
    • Isolation and characterization of hirudin isoinhibitors and sequence analysis of hirudin PA
    • Dodt, J., Machleidt, W., Seemüller, U., Maschler, R. and Fritz, H. 1986. Isolation and characterization of hirudin isoinhibitors and sequence analysis of hirudin PA. Biol. Chem. Hoppe-Seyler 367: 803-811.
    • (1986) Biol. Chem. Hoppe-Seyler , vol.367 , pp. 803-811
    • Dodt, J.1    Machleidt, W.2    Seemüller, U.3    Maschler, R.4    Fritz, H.5
  • 7
    • 0027432559 scopus 로고
    • Purification and characterization of inhibitors of blood coagulation factor Xa from hematophagous organisms
    • Dunwiddie, C.T., Waxman, L., Vlasuk, G.P. and Friedman, P.A. 1993. Purification and characterization of inhibitors of blood coagulation factor Xa from hematophagous organisms. Methods Enzymol. 223: 291-321.
    • (1993) Methods Enzymol. , vol.223 , pp. 291-321
    • Dunwiddie, C.T.1    Waxman, L.2    Vlasuk, G.P.3    Friedman, P.A.4
  • 8
    • 0029248203 scopus 로고
    • Identification of anticoagulant activities in the salivary glands of the soft tick, Ornithodoros savignyi
    • Gaspar, A.R.M.D., Crause, J.C. and Neitz, A.W.H. 1995. Identification of anticoagulant activities in the salivary glands of the soft tick, Ornithodoros savignyi. Exp. Appl. Acarol. 19: 117-126.
    • (1995) Exp. Appl. Acarol. , vol.19 , pp. 117-126
    • Gaspar, A.R.M.D.1    Crause, J.C.2    Neitz, A.W.H.3
  • 10
    • 0015546107 scopus 로고
    • Determination of the operational molarity of solutions of bovine α-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorometric titration
    • Jameson, G.W., Roberts, D.V., Adams, R.W., Kyle, W.S.A. and Elmore, D.T. 1973. Determination of the operational molarity of solutions of bovine α-chymotrypsin, trypsin, thrombin and factor Xa by spectrofluorometric titration. Biochem. J. 131: 107-117.
    • (1973) Biochem. J. , vol.131 , pp. 107-117
    • Jameson, G.W.1    Roberts, D.V.2    Adams, R.W.3    Kyle, W.S.A.4    Elmore, D.T.5
  • 11
    • 0025683260 scopus 로고
    • Tick anticoagulant peptide: Kinetic analysis of the recombinant inhibitor with blood coagulation factor Xa
    • Jordan, S.P., Waxman, L., Smith, D.E. and Vlasuk, G.P. 1990. Tick anticoagulant peptide: kinetic analysis of the recombinant inhibitor with blood coagulation factor Xa. Biochemistry 29: 11095-11100.
    • (1990) Biochemistry , vol.29 , pp. 11095-11100
    • Jordan, S.P.1    Waxman, L.2    Smith, D.E.3    Vlasuk, G.P.4
  • 12
    • 0029242515 scopus 로고
    • Isolation and characterization of an anticoagulant present in the salivary glands of the bont-legged tick Hyalomma truncatum
    • Joubert, A.M., Crause, J.C., Gaspar, A.R.M.D., Clarke, F.C., Spickett, A.M. and Neitz, A.W.H. 1995. Isolation and characterization of an anticoagulant present in the salivary glands of the bont-legged tick Hyalomma truncatum. Exp. Appl. Acarol. 19: 79-92.
    • (1995) Exp. Appl. Acarol. , vol.19 , pp. 79-92
    • Joubert, A.M.1    Crause, J.C.2    Gaspar, A.R.M.D.3    Clarke, F.C.4    Spickett, A.M.5    Neitz, A.W.H.6
  • 13
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons
    • Karas, M. and Hillenkamp, F. 1988. Laser desorption ionization of proteins with molecular masses exceeding 10 000 daltons. Anal. Chem. 60: 2299-2301.
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 14
    • 0016778913 scopus 로고
    • Fibrinolytic substance (hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto 1920)
    • Kelen, E.M.A. and Rosenfeld, G. 1975. Fibrinolytic substance (hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto 1920). Haemostasis 4: 51-64.
    • (1975) Haemostasis , vol.4 , pp. 51-64
    • Kelen, E.M.A.1    Rosenfeld, G.2
  • 15
    • 0026162879 scopus 로고
    • Purification and characterization of an anticoagulant from the salivary glands of the ixodid tick Rhipicephalus appendiculatus
    • Limo, M.K., Voigt, W.P., Tumbo-Oeri, A.G., Njogu, R.M. and Ole-Moi Yoi, O.K. 1991. Purification and characterization of an anticoagulant from the salivary glands of the ixodid tick Rhipicephalus appendiculatus. Exp. Parasitol. 72: 418-429.
    • (1991) Exp. Parasitol. , vol.72 , pp. 418-429
    • Limo, M.K.1    Voigt, W.P.2    Tumbo-Oeri, A.G.3    Njogu, R.M.4    Ole-Moi Yoi, O.K.5
  • 16
    • 0021359565 scopus 로고
    • Hementin: Anticoagulant protease from the salivary gland of the leech Haementeria ghilianni
    • Malinconico, S.M., Katz, J.B. and Budzynski, A.Z. 1984a. Hementin: anticoagulant protease from the salivary gland of the leech Haementeria ghilianni. J. Lab. Clin. Med. 102: 44-58.
    • (1984) J. Lab. Clin. Med. , vol.102 , pp. 44-58
    • Malinconico, S.M.1    Katz, J.B.2    Budzynski, A.Z.3
  • 17
    • 0021682646 scopus 로고
    • Fibrinogen degradation by hementin, a fribrinogenolytic anticoagulant from the salivary glands of the leech Haementeria ghilianni
    • Malinconico, S.M., Katz, J.B. and Budzynski, A.Z. 1984b. Fibrinogen degradation by hementin, a fribrinogenolytic anticoagulant from the salivary glands of the leech Haementeria ghilianni. J. Lab. Clin. Med. 104: 842-854.
    • (1984) J. Lab. Clin. Med. , vol.104 , pp. 842-854
    • Malinconico, S.M.1    Katz, J.B.2    Budzynski, A.Z.3
  • 18
    • 0000319455 scopus 로고
    • Hirudin as an inhibitor of thrombin
    • Markwardt, F. 1970. Hirudin as an inhibitor of thrombin. Methods Enzymol. 19: 924-932.
    • (1970) Methods Enzymol. , vol.19 , pp. 924-932
    • Markwardt, F.1
  • 19
    • 0028114116 scopus 로고
    • Inventory of coagulation inhibitors of animals feeding on blood
    • Markwardt, F. 1994. Inventory of coagulation inhibitors of animals feeding on blood. Thromb. Haemostasis 72: 477-480.
    • (1994) Thromb. Haemostasis , vol.72 , pp. 477-480
    • Markwardt, F.1
  • 20
    • 0014454095 scopus 로고
    • Kinetics of reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors
    • Morrison, J.F. 1969. Kinetics of reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors. Biochim. Biophys. Acta 185: 269-286.
    • (1969) Biochim. Biophys. Acta , vol.185 , pp. 269-286
    • Morrison, J.F.1
  • 21
    • 0001396685 scopus 로고
    • The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions
    • Morrison, J.F. 1982. The slow-binding and slow, tight-binding inhibition of enzyme-catalysed reactions. Trends Biochem. Sci. 7: 102-105.
    • (1982) Trends Biochem. Sci. , vol.7 , pp. 102-105
    • Morrison, J.F.1
  • 22
    • 0141474501 scopus 로고
    • Plasma proteins, immunoglobulins and blood coagulation
    • Appleton and Lange
    • Murray, R.K., Granner, D.K., Mayes, P.A. and Rodwell, V.W. 1993. Plasma proteins, immunoglobulins and blood coagulation. In Harper's biochemistry, pp. 677-687. Appleton and Lange.
    • (1993) Harper's Biochemistry , pp. 677-687
    • Murray, R.K.1    Granner, D.K.2    Mayes, P.A.3    Rodwell, V.W.4
  • 24
    • 0023174943 scopus 로고
    • Role of saliva in blood-feeding by arthropods
    • Ribeiro, J.M.C. 1987. Role of saliva in blood-feeding by arthropods. Ann. Rev. Entomol. 32: 463-478.
    • (1987) Ann. Rev. Entomol. , vol.32 , pp. 463-478
    • Ribeiro, J.M.C.1
  • 25
    • 0024465384 scopus 로고
    • Primary structure of new iso-hirudins
    • Scharf, M., Engels, J. and Tripier, D. 1989. Primary structure of new iso-hirudins. FEBS Lett. 255: 105-110.
    • (1989) FEBS Lett. , vol.255 , pp. 105-110
    • Scharf, M.1    Engels, J.2    Tripier, D.3
  • 27
    • 0025264334 scopus 로고
    • The role of vector saliva in transmission of arthropod-borne disease
    • Titus, R.C. and Ribeiro, J.M.C. 1990. The role of vector saliva in transmission of arthropod-borne disease. Parasitol. Today 6: 157-160.
    • (1990) Parasitol. Today , vol.6 , pp. 157-160
    • Titus, R.C.1    Ribeiro, J.M.C.2
  • 28
    • 0026527512 scopus 로고
    • Restriction fragment length polymorphism analysis of ERBB2 oncogene by capillary electrophoresis
    • Ulfelder, K.J., Schwartz, H.E., Hall, J.M. and Sunzeri, F.J. 1992. Restriction fragment length polymorphism analysis of ERBB2 oncogene by capillary electrophoresis. Anal. Biochem. 200: 260-267.
    • (1992) Anal. Biochem. , vol.200 , pp. 260-267
    • Ulfelder, K.J.1    Schwartz, H.E.2    Hall, J.M.3    Sunzeri, F.J.4
  • 29
    • 0027418305 scopus 로고
    • Isolation of an inhibitor selective for collagen-stimulated platelet aggregation from the soft tick Ornithodoros moubata
    • Waxman, L. and Connolly, T.M. 1993. Isolation of an inhibitor selective for collagen-stimulated platelet aggregation from the soft tick Ornithodoros moubata. J. Biol. Chem. 268: 5445-5449.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5445-5449
    • Waxman, L.1    Connolly, T.M.2
  • 30
    • 0025375504 scopus 로고
    • Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa
    • Waxman, L., Smith, D.E., Arcuri, K.E. and Vlasuk, P. 1990. Tick anticoagulant peptide (TAP) is a novel inhibitor of blood coagulation factor Xa. Science 248: 593-596.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, P.4
  • 31
    • 0018699952 scopus 로고
    • The kinetics of reversible tight-binding inhibition
    • Williams, J.W. and Morrison, J.F. 1979. The kinetics of reversible tight-binding inhibition. Methods Enzymol. 63: 437-467.
    • (1979) Methods Enzymol. , vol.63 , pp. 437-467
    • Williams, J.W.1    Morrison, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.