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Volumn 22, Issue 3, 1996, Pages 273-278

Platelet aggregation and coagulation inhibitors in leech saliva and their roles in leech therapy

Author keywords

Apyrase; Collagenase; Hirudin; Leech; PAF antagonist

Indexed keywords

ADENOSINE DIPHOSPHATE; ADRENALIN; APYRASE; BLOOD CLOTTING INHIBITOR; COLLAGEN; HIRUDIN; THROMBIN; THROMBOCYTE ACTIVATING FACTOR;

EID: 0029924721     PISSN: 00946176     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-2007-999019     Document Type: Review
Times cited : (36)

References (69)
  • 2
    • 84924926451 scopus 로고
    • La renovation d'une medication desuète: Les sangsues
    • Durand F: La renovation d'une medication desuète: Les sangsues. Arch Intern Neurol 69:17-27, 41-47, 1950.
    • (1950) Arch Intern Neurol , vol.69 , pp. 17-27
    • Durand, F.1
  • 3
    • 0001146972 scopus 로고
    • On the action of a secretion obtained from the medical leech on the coagulation of the blood
    • Haycraft JB: On the action of a secretion obtained from the medical leech on the coagulation of the blood. Proc R Soc Lond 36:478-487, 1884.
    • (1884) Proc R Soc Lond , vol.36 , pp. 478-487
    • Haycraft, J.B.1
  • 4
    • 0000319455 scopus 로고
    • Hirudin as an inhibitor of thrombin
    • Markwardt F: Hirudin as an inhibitor of thrombin. Methods Enzymol 19:924-932, 1970.
    • (1970) Methods Enzymol , vol.19 , pp. 924-932
    • Markwardt, F.1
  • 5
    • 0000935703 scopus 로고
    • Large scale preparation of hirudin
    • Bagdy D, E Barabas, L Graf: Large scale preparation of hirudin. Thromb Res 2:229-238, 1973.
    • (1973) Thromb Res , vol.2 , pp. 229-238
    • Bagdy, D.1    Barabas, E.2    Graf, L.3
  • 6
    • 0021024613 scopus 로고
    • The functional domain of hirudin, a thrombin-specific inhibitor
    • Chang JY: The functional domain of hirudin, a thrombin-specific inhibitor. FEBS Lett 264:307-313, 1983.
    • (1983) FEBS Lett , vol.264 , pp. 307-313
    • Chang, J.Y.1
  • 7
    • 0021331392 scopus 로고
    • The complete amino acid sequence of hirudin, a thrombin specific inhibitor
    • Dodt J, HP Müller, U Seemüller, JY Chang: The complete amino acid sequence of hirudin, a thrombin specific inhibitor. FEBS Lett 165:180-184, 1984.
    • (1984) FEBS Lett , vol.165 , pp. 180-184
    • Dodt, J.1    Müller, H.P.2    Seemüller, U.3    Chang, J.Y.4
  • 8
    • 0013586606 scopus 로고
    • The conformation of hirudin in solution: A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics
    • Clore GM, DR Sukumaran, M Nilges, J Zarbock, AM Gronenborn: The conformation of hirudin in solution: A study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J 6:529-537, 1987.
    • (1987) EMBO J , vol.6 , pp. 529-537
    • Clore, G.M.1    Sukumaran, D.R.2    Nilges, M.3    Zarbock, J.4    Gronenborn, A.M.5
  • 10
    • 8944262862 scopus 로고
    • First International Symposium on Hirudin. Frankfurt A.M. 23-24 June 1989
    • Munich
    • First International Symposium on Hirudin. Frankfurt A.M. 23-24 June 1989. (Abst.) Angio Arch (Munich) 18:1-104, 1989.
    • (1989) Angio Arch , vol.18 , pp. 1-104
  • 12
    • 0022762461 scopus 로고
    • Chemical synthesis and expression of a gene coding for hirudin, the thrombin-specific inhibitor from the leech Hirudo medicinalis
    • Bergmann C, J Dodt, S Kohler, E Fink, HG Ciassen: Chemical synthesis and expression of a gene coding for hirudin, the thrombin-specific inhibitor from the leech Hirudo medicinalis. Biol Chem Hoppe-Seyler 367:731-740, 1986.
    • (1986) Biol Chem Hoppe-Seyler , vol.367 , pp. 731-740
    • Bergmann, C.1    Dodt, J.2    Kohler, S.3    Fink, E.4    Ciassen, H.G.5
  • 13
    • 0022543853 scopus 로고
    • Expression, secretion and processing of hirudin in E. coli using the alkaline phosphatase signal sequence
    • Dodt J, T Shmitz, T Schafer, C Bergmann: Expression, secretion and processing of hirudin in E. coli using the alkaline phosphatase signal sequence. FEBS Lett 202:373-377, 1986.
    • (1986) FEBS Lett , vol.202 , pp. 373-377
    • Dodt, J.1    Shmitz, T.2    Schafer, T.3    Bergmann, C.4
  • 14
    • 0027527503 scopus 로고
    • Hirudin and hirudin-based peptides
    • Stone SR, JM Maraganore: Hirudin and hirudin-based peptides. Methods Enzymol 223:312-336, 1993.
    • (1993) Methods Enzymol , vol.223 , pp. 312-336
    • Stone, S.R.1    Maraganore, J.M.2
  • 15
    • 0000843601 scopus 로고
    • The production of hyaluronate oligosaccharides by leech hyaluronidase and alkali
    • Linker A, K Meyer, P Hoffman: The production of hyaluronate oligosaccharides by leech hyaluronidase and alkali. J Biol Chem 235:924-927, 1960.
    • (1960) J Biol Chem , vol.235 , pp. 924-927
    • Linker, A.1    Meyer, K.2    Hoffman, P.3
  • 16
    • 0000998762 scopus 로고
    • Purification and characterization of leech hyaluronic acid - Endo-β-glucuronidase
    • Yuki H, WH Fishman: Purification and characterization of leech hyaluronic acid - endo-β-glucuronidase. J Biol Chem 238:1877-1879, 1963.
    • (1963) J Biol Chem , vol.238 , pp. 1877-1879
    • Yuki, H.1    Fishman, W.H.2
  • 18
    • 0001284291 scopus 로고
    • Proteinase inhibitors of the leech Hirudo medicinalis (hirudins, bdellins, eglins)
    • Barrett AJ, G Salvesen (eds): Elsevier, Amsterdam
    • Seemüller U, J Dodt, E Fink, H Fritz: Proteinase inhibitors of the leech Hirudo medicinalis (hirudins, bdellins, eglins). In: Barrett AJ, G Salvesen (eds): Proteinase Inhibitors. Elsevier, Amsterdam, 1986, pp 337-352.
    • (1986) Proteinase Inhibitors , pp. 337-352
    • Seemüller, U.1    Dodt, J.2    Fink, E.3    Fritz, H.4
  • 19
    • 0020639964 scopus 로고
    • Avulsion of the scalp treated by microvascular repair: The use of leeches for post-operative decongestion
    • Henderson HP, B Matti, AG Laing, S Morelli, L Sully: Avulsion of the scalp treated by microvascular repair: The use of leeches for post-operative decongestion. Br J Plast Surg 36:235-239, 1983.
    • (1983) Br J Plast Surg , vol.36 , pp. 235-239
    • Henderson, H.P.1    Matti, B.2    Laing, A.G.3    Morelli, S.4    Sully, L.5
  • 20
    • 0020530653 scopus 로고
    • The medicinal leech and its use in plastic surgery: A possible cause for infection
    • Whitlock MR, PM O'Hare, R Sanders, NC Morrow: The medicinal leech and its use in plastic surgery: A possible cause for infection. Br J Plast Surg 36:240-244, 1983.
    • (1983) Br J Plast Surg , vol.36 , pp. 240-244
    • Whitlock, M.R.1    O'Hare, P.M.2    Sanders, R.3    Morrow, N.C.4
  • 21
  • 22
    • 0023630328 scopus 로고
    • The saliva of the medicinal leech Hirudo medicinalis II. Inhibition of platelet aggregation and of leukocyte activity and examination of reputed anaesthetic effects
    • Rigbi M, H Levy, A Eldor, F Iraqi, M Teitelbaum, M Orevi, A Horovitz, R Galun: The saliva of the medicinal leech Hirudo medicinalis II. Inhibition of platelet aggregation and of leukocyte activity and examination of reputed anaesthetic effects. Comp Biochem Physiol [C] 88:95-98, 1987.
    • (1987) Comp Biochem Physiol [C] , vol.88 , pp. 95-98
    • Rigbi, M.1    Levy, H.2    Eldor, A.3    Iraqi, F.4    Teitelbaum, M.5    Orevi, M.6    Horovitz, A.7    Galun, R.8
  • 24
    • 8944241802 scopus 로고
    • Platelet aggregation inhibitors in Hirudo medicinalis leech saliva: Partial purification and characterization by their effect on different platelet agonists
    • Orevi M, M Rigbi, A Horovitz, A Eldor: Platelet aggregation inhibitors in Hirudo medicinalis leech saliva: Partial purification and characterization by their effect on different platelet agonists. (Abst.) Blood 70(suppl. 1): 357a, 1987.
    • (1987) Blood , vol.70 , Issue.1 SUPPL.
    • Orevi, M.1    Rigbi, M.2    Horovitz, A.3    Eldor, A.4
  • 25
    • 0021438219 scopus 로고
    • Salivary gland secretion of the leech Hirudo medicinalis inhibits ADP-induced human platelet adhesion on a collagen coated surface
    • English translation by Plenum Press
    • Baskova IP, F Misselwitz, GI Nikonov, ID Novikov, VL Leitin, VS Repin: Salivary gland secretion of the leech Hirudo medicinalis inhibits ADP-induced human platelet adhesion on a collagen coated surface. Biol Eksp Biol Med 97:696-771, 1984. (English translation by Plenum Press.)
    • (1984) Biol Eksp Biol Med , vol.97 , pp. 696-771
    • Baskova, I.P.1    Misselwitz, F.2    Nikonov, G.I.3    Novikov, I.D.4    Leitin, V.L.5    Repin, V.S.6
  • 27
    • 0026523380 scopus 로고
    • A potent inhibitor of platelet activating factor from the saliva of the leech Hirudo medicinalis
    • Orevi M, M Rigbi, E Hy-Am, Y Matzner, A Eldor: A potent inhibitor of platelet activating factor from the saliva of the leech Hirudo medicinalis. Prostaglandins 43:483-495, 1992.
    • (1992) Prostaglandins , vol.43 , pp. 483-495
    • Orevi, M.1    Rigbi, M.2    Hy-Am, E.3    Matzner, Y.4    Eldor, A.5
  • 28
    • 0018569247 scopus 로고
    • 1, and guanine nucleotides
    • 1, and guanine nucleotides. J Biol Chem 254:10731-10797, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 10731-10797
    • Steer, M.L.1    Wood, A.2
  • 29
    • 0018804588 scopus 로고
    • ADP is a potent inhibitor of human platelet plasma membrane adenylate cyclase
    • Cooper DMF, M Rodbell: ADP is a potent inhibitor of human platelet plasma membrane adenylate cyclase. Nature 282:515-518, 1979.
    • (1979) Nature , vol.282 , pp. 515-518
    • Cooper, D.M.F.1    Rodbell, M.2
  • 30
    • 0026724312 scopus 로고
    • Biochemical insights derived from insect diversity
    • Law JH, Ribeiro JMC, MA Wells: Biochemical insights derived from insect diversity. Annu Rev Biochem 67:87-111, 1992.
    • (1992) Annu Rev Biochem , vol.67 , pp. 87-111
    • Law, J.H.1    Ribeiro, J.M.C.2    Wells, M.A.3
  • 31
    • 0019494126 scopus 로고
    • Platelet antiaggregating activity in the salivary secretion of the blood-sucking bug Rhodnius prolixus
    • Ribeiro JMC, ES Garcia: Platelet antiaggregating activity in the salivary secretion of the blood-sucking bug Rhodnius prolixus. Experientia 37:384-386, 1981.
    • (1981) Experientia , vol.37 , pp. 384-386
    • Ribeiro, J.M.C.1    Garcia, E.S.2
  • 32
    • 0022555858 scopus 로고
    • Platelet activating factor: A biologically active phosphoglyceride
    • Hanahan DJ: Platelet activating factor: A biologically active phosphoglyceride. Annu Rev Biochem 55:435-510, 1986.
    • (1986) Annu Rev Biochem , vol.55 , pp. 435-510
    • Hanahan, D.J.1
  • 34
    • 0025263965 scopus 로고
    • Platelet activating factor may act as a second messenger in the release of icosanoids and superoxide anions from leukocytes and endothelial cells
    • Stewart, AG, PN Dubbin, T Harris, GJ Dusting: Platelet activating factor may act as a second messenger in the release of icosanoids and superoxide anions from leukocytes and endothelial cells. Proc Natl Acad Sci USA 87:3215-3219, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3215-3219
    • Stewart, A.G.1    Dubbin, P.N.2    Harris, T.3    Dusting, G.J.4
  • 35
    • 0343188495 scopus 로고
    • Platelet-activating factors, neutrophil granulocyte function and BN52021
    • Braquet P (Ed): JR Prous Science Publishers, Barcelona
    • Filep J, E Foldes-Filep: Platelet-activating factors, neutrophil granulocyte function and BN52021. In: Braquet P (Ed): Gingkolides - Chemistry, Biology, Pharmacology and Clinical Perspectives. JR Prous Science Publishers, Barcelona, 1988, pp 151-159.
    • (1988) Gingkolides - Chemistry, Biology, Pharmacology and Clinical Perspectives , pp. 151-159
    • Filep, J.1    Foldes-Filep, E.2
  • 36
    • 0025329916 scopus 로고
    • Decorsin: A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora
    • Seymour JL, WJ Henzel, B Nevins, JT Strels, RA Lazarus: Decorsin: A potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor from the leech Macrobdella decora. J Biol Chem 266:10143-10147, 1990.
    • (1990) J Biol Chem , vol.266 , pp. 10143-10147
    • Seymour, J.L.1    Henzel, W.J.2    Nevins, B.3    Strels, J.T.4    Lazarus, R.A.5
  • 40
    • 0026493769 scopus 로고
    • Inhibition of plasma kallikrein, kininase and kinin-like activities from preparations of medicinal leeches
    • Baskova IP, S Khalil, VF Nartikova, TS Pashkina: Inhibition of plasma kallikrein, kininase and kinin-like activities from preparations of medicinal leeches. Thromb Res 67:721-730, 1992.
    • (1992) Thromb Res , vol.67 , pp. 721-730
    • Baskova, I.P.1    Khalil, S.2    Nartikova, V.F.3    Pashkina, T.S.4
  • 41
    • 0026102550 scopus 로고
    • Destabilase, the novel ∈-(γ-Glu)-Lys isopeptidase with thrombolytic activity
    • Baskova IP, GI Nikonov: Destabilase, the novel ∈-(γ-Glu)-Lys isopeptidase with thrombolytic activity. Blood Coagul Fibrinolysis 2:167-172, 1992.
    • (1992) Blood Coagul Fibrinolysis , vol.2 , pp. 167-172
    • Baskova, I.P.1    Nikonov, G.I.2
  • 42
    • 0027303651 scopus 로고
    • Monomerization of fraction DD by destabilase from the medicinal leech does not alter the N-terminal sequence of the γ-chain
    • Zavalova LL, EV Kuzina, LB Levina, IP Baskova: Monomerization of fraction DD by destabilase from the medicinal leech does not alter the N-terminal sequence of the γ-chain. Thromb Res 71:241-244, 1994.
    • (1994) Thromb Res , vol.71 , pp. 241-244
    • Zavalova, L.L.1    Kuzina, E.V.2    Levina, L.B.3    Baskova, I.P.4
  • 43
    • 0027478758 scopus 로고
    • Purification and characterization of a novel zinc-proteinase from cultures of Aeromonas hydrophila
    • Loewy AG, U Santer, M Wieczorek, JK Blodgett, WS Jones, JC Cheronis: Purification and characterization of a novel zinc-proteinase from cultures of Aeromonas hydrophila. J Biol Chem 268:9071-9078, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 9071-9078
    • Loewy, A.G.1    Santer, U.2    Wieczorek, M.3    Blodgett, J.K.4    Jones, W.S.5    Cheronis, J.C.6
  • 44
    • 0023189460 scopus 로고
    • Isolation and characterization of antistasin
    • Tuszynski GP, TB Gasic, GJ Gasic: Isolation and characterization of antistasin. J Biol Chem 262:9718-9723, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 9718-9723
    • Tuszynski, G.P.1    Gasic, T.B.2    Gasic, G.J.3
  • 45
    • 0024445042 scopus 로고
    • Antistasin, a leech-derived inhibitor of Factor Xa kinetic analysis of enzyme inhibition and identification of the reactive site
    • Dunwiddie C, NA Thornberry, HG Bull, M Sardana, PA Friedman, JW Jacobs, E Simpson: Antistasin, a leech-derived inhibitor of Factor Xa kinetic analysis of enzyme inhibition and identification of the reactive site. J Biol Chem 264:16694-16699, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 16694-16699
    • Dunwiddie, C.1    Thornberry, N.A.2    Bull, H.G.3    Sardana, M.4    Friedman, P.A.5    Jacobs, J.W.6    Simpson, E.7
  • 46
    • 0026497653 scopus 로고
    • Site-directed mutagenesis of the leech derived factor Xa inhibitor antistasin. Probing the reactive site
    • Hofmann KJ, EM Nutt, CT Dunwiddie: Site-directed mutagenesis of the leech derived factor Xa inhibitor antistasin. Probing the reactive site. Biochem J 287(pt 3):943-949, 1992.
    • (1992) Biochem J , vol.287 , Issue.3 PART , pp. 943-949
    • Hofmann, K.J.1    Nutt, E.M.2    Dunwiddie, C.T.3
  • 47
    • 0026639859 scopus 로고
    • Heparin binding properties of the carboxyl terminal domain of [A 103, 106, 108] antistasin 93-119
    • Manley GD, TJ Owen, JL Krstenansky, RG Brankamp, AD Cardin: Heparin binding properties of the carboxyl terminal domain of [A 103, 106, 108] antistasin 93-119. Adv Exp Med Biol 313:135-140, 1992.
    • (1992) Adv Exp Med Biol , vol.313 , pp. 135-140
    • Manley, G.D.1    Owen, T.J.2    Krstenansky, J.L.3    Brankamp, R.G.4    Cardin, A.D.5
  • 48
    • 0027201975 scopus 로고
    • Crystallization and preliminary crystallographic analysis of antistasin, a leech-derived inhibitor of blood coagulation factor Xa
    • Schreuder H, A Arkema, B de Boer, K Kalk, R Dijkema, J Mulders, H Theunissen, W Hol: Crystallization and preliminary crystallographic analysis of antistasin, a leech-derived inhibitor of blood coagulation factor Xa. J Mol Biol 231:1137-1138, 1993.
    • (1993) J Mol Biol , vol.231 , pp. 1137-1138
    • Schreuder, H.1    Arkema, A.2    De Boer, B.3    Kalk, K.4    Dijkema, R.5    Mulders, J.6    Theunissen, H.7    Hol, W.8
  • 49
    • 0027432559 scopus 로고
    • Purification and characterization of blood coagulation factor Xa from hematophagous organisms
    • Dunwiddie CT, L Waxman, GP Vlasuk, PA Friedman: Purification and characterization of blood coagulation factor Xa from hematophagous organisms. Methods Enzymol 223:291-312, 1993.
    • (1993) Methods Enzymol , vol.223 , pp. 291-312
    • Dunwiddie, C.T.1    Waxman, L.2    Vlasuk, G.P.3    Friedman, P.A.4
  • 51
    • 0027218540 scopus 로고
    • Anticoagulant potential of synthetic and recombinant inhibitors of factor Xa and thrombin in vitro
    • Hauptmann J, B Kaiser: Anticoagulant potential of synthetic and recombinant inhibitors of factor Xa and thrombin in vitro. Blood Coagul Fibrinolysis 4:577-582, 1993.
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 577-582
    • Hauptmann, J.1    Kaiser, B.2
  • 53
    • 0024321427 scopus 로고
    • Isolation and structural characterization of coagulation Factor Xa from Leech Haementeria ghilianii
    • Condra C, E Nutt, CJ Petraski, E Simpson, PA Friedman, JW Jacobs: Isolation and structural characterization of coagulation Factor Xa from Leech Haementeria ghilianii: Thromb Haemostas 61:437-441, 1989.
    • (1989) Thromb Haemostas , vol.61 , pp. 437-441
    • Condra, C.1    Nutt, E.2    Petraski, C.J.3    Simpson, E.4    Friedman, P.A.5    Jacobs, J.W.6
  • 54
    • 0027972373 scopus 로고
    • Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis
    • Söllner C, B Mentele, C Eckerskorn, H Fritz, CP Sommerhoff: Isolation and characterization of hirustasin, an antistasin-type serine-proteinase inhibitor from the medical leech Hirudo medicinalis. Eur J Biochem 219:937-943, 1994.
    • (1994) Eur J Biochem , vol.219 , pp. 937-943
    • Söllner, C.1    Mentele, B.2    Eckerskorn, C.3    Fritz, H.4    Sommerhoff, C.P.5
  • 55
    • 0019865446 scopus 로고
    • Anticoagulant and antifibrinolytic properties of salivary proteins from the leech Haementeria ghilianii
    • Budzynski AZ, SA Olexa, BS Brizuela, RT Sawyer, GS Stent: Anticoagulant and antifibrinolytic properties of salivary proteins from the leech Haementeria ghilianii. Proc Soc Exp Biol Med 168:266-275, 1981.
    • (1981) Proc Soc Exp Biol Med , vol.168 , pp. 266-275
    • Budzynski, A.Z.1    Olexa, S.A.2    Brizuela, B.S.3    Sawyer, R.T.4    Stent, G.S.5
  • 56
    • 0020577709 scopus 로고
    • Inhibition of lung tumor colonization by leech salivary gland extracts from Haementeria ghilianii
    • Gusic GJ, ED Viner, AZ Budzynski, GP Gasic. Inhibition of lung tumor colonization by leech salivary gland extracts from Haementeria ghilianii. Cancer Res 43:1633-1635, 1983.
    • (1983) Cancer Res , vol.43 , pp. 1633-1635
    • Gusic, G.J.1    Viner, E.D.2    Budzynski, A.Z.3    Gasic, G.P.4
  • 57
    • 0016778913 scopus 로고
    • Fibrinogenolytic substance (hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto [1920])
    • Kelen EMA, G Rosenfeld: Fibrinogenolytic substance (hementerin) of Brazilian blood-sucking leeches (Haementeria lutzi Pinto [1920]). Haemostasis 4:51-64, 1975.
    • (1975) Haemostasis , vol.4 , pp. 51-64
    • Kelen, E.M.A.1    Rosenfeld, G.2
  • 58
    • 0025375504 scopus 로고
    • The tick anticoagulant peptide (TAP) is a novel inhibitor of factor Xa
    • Waxman L, DE Smith, KE Arcuri, GP Vlasuk: The tick anticoagulant peptide (TAP) is a novel inhibitor of factor Xa. Science 248:593-596, 1990.
    • (1990) Science , vol.248 , pp. 593-596
    • Waxman, L.1    Smith, D.E.2    Arcuri, K.E.3    Vlasuk, G.P.4
  • 59
    • 0025683260 scopus 로고
    • Tick anticoagulant peptide: Kinetic analysis of recombinant inhibitor with blood coagulation factor Xa
    • Jordan SP, L Waxman, DE Smith, GP Vlasuk: Tick anticoagulant peptide: kinetic analysis of recombinant inhibitor with blood coagulation factor Xa. Biochemistry 29:11095-11100, 1990.
    • (1990) Biochemistry , vol.29 , pp. 11095-11100
    • Jordan, S.P.1    Waxman, L.2    Smith, D.E.3    Vlasuk, G.P.4
  • 60
    • 0027295989 scopus 로고
    • Antithrombotic activity of recombinant tick anticoagulant peptide and heparin in a rabbit model of venous thrombosis
    • Fioravanti C, D Burkholder, B Francis, PK Siegel, RE Gibson: Antithrombotic activity of recombinant tick anticoagulant peptide and heparin in a rabbit model of venous thrombosis. Thromb Res 71:317-324, 1993.
    • (1993) Thromb Res , vol.71 , pp. 317-324
    • Fioravanti, C.1    Burkholder, D.2    Francis, B.3    Siegel, P.K.4    Gibson, R.E.5
  • 61
    • 0025017989 scopus 로고
    • Isolation and characterizaiton of a coagulation factor Xa inhibitor from black fly salivary glands
    • Jacobs JW, EW Cupp, M Sardana, PA Friedman: Isolation and characterizaiton of a coagulation factor Xa inhibitor from black fly salivary glands. Thromb Haemostas 64:235-238, 1990.
    • (1990) Thromb Haemostas , vol.64 , pp. 235-238
    • Jacobs, J.W.1    Cupp, E.W.2    Sardana, M.3    Friedman, P.A.4
  • 62
    • 8944258144 scopus 로고
    • Effect of tsetse salivary gland homogenate on coagulation and fibrinolysis
    • Parker KR, MJ Mant: Effect of tsetse salivary gland homogenate on coagulation and fibrinolysis. Thromb Haemostas 42:723-751, 1979.
    • (1979) Thromb Haemostas , vol.42 , pp. 723-751
    • Parker, K.R.1    Mant, M.J.2
  • 63
    • 0025869583 scopus 로고
    • Factors V and VII anticoagulant activities in the salivary glands of feeding Dermacentor andersoni ticks
    • Gordon JR, JR Allen JR: Factors V and VII anticoagulant activities in the salivary glands of feeding Dermacentor andersoni ticks. J Parasitol 77:167-170, 1991.
    • (1991) J Parasitol , vol.77 , pp. 167-170
    • Gordon Jr., J.R.1    Allen, J.R.2
  • 64
    • 0013850303 scopus 로고
    • Prolixin-S and prolixin-G: Two anticoagulants from Rhodnius prolixus Stahl
    • Hellman K, R Hawkins: Prolixin-S and prolixin-G: two anticoagulants from Rhodnius prolixus Stahl. Nature 207:265-267, 1965.
    • (1965) Nature , vol.207 , pp. 265-267
    • Hellman, K.1    Hawkins, R.2
  • 65
    • 0027155257 scopus 로고
    • The Ancylostoma factor Xa inhibitor: Partial purification and its identification as a major hookworm-derived anticoagulant in vitro
    • Cappelo M, LP Clyne, P McPhedran, PJ Hotez: The Ancylostoma factor Xa inhibitor: partial purification and its identification as a major hookworm-derived anticoagulant in vitro. J Infect Dis 167:1474-1477, 1993.
    • (1993) J Infect Dis , vol.167 , pp. 1474-1477
    • Cappelo, M.1    Clyne, L.P.2    McPhedran, P.3    Hotez, P.J.4
  • 66
    • 0027452108 scopus 로고
    • Vampire bat salivary plasminogen activator
    • Gardell SJ, PA Friedman: Vampire bat salivary plasminogen activator. Methods Enzymol 223:233-249, 1993.
    • (1993) Methods Enzymol , vol.223 , pp. 233-249
    • Gardell, S.J.1    Friedman, P.A.2
  • 68
    • 8944221229 scopus 로고
    • Digit replantation applying the leech Hirudo medicinalis
    • Brody GA, WJ Mahoney, VR Hentz: Digit replantation applying the leech Hirudo medicinalis. Clin Orthop 133:245-249, 1989.
    • (1989) Clin Orthop , vol.133 , pp. 245-249
    • Brody, G.A.1    Mahoney, W.J.2    Hentz, V.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.