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Volumn 52, Issue 13, 1992, Pages 3622-3628

Characterization and Purification of a Guanidinobenzoatase: A Possible Marker of Human Renal Carcinoma

Author keywords

[No Author keywords available]

Indexed keywords

GUANIDINE DERIVATIVE; GUANIDINOBENZOATASE; SERINE PROTEINASE INHIBITOR; TUMOR MARKER; UNCLASSIFIED DRUG;

EID: 0026623041     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (18)

References (30)
  • 2
    • 0023746649 scopus 로고
    • Membrane and matrix localization of proteinases: a common theme in tumor cell invasion and angiogenesis
    • MoscateUi, D., and Rifkin, D. B. Membrane and matrix localization of proteinases: a common theme in tumor cell invasion and angiogenesis. Biochim. Biophys. Acta, 948:67-85,1988.
    • (1988) Biochim. Biophys. Acta , vol.948 , pp. 67-85
    • MoscateUi, D.1    Rifkin, D.B.2
  • 3
    • 0026027556 scopus 로고
    • Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation
    • Liotta, L. A., Steeg, P. S., and Stetler-Stevenson, W. G. Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation. Cell, 64: 327-336,1991.
    • (1991) Cell , vol.64 , pp. 327-336
    • Liotta, L.A.1    Steeg, P.S.2    Stetler-Stevenson, W.G.3
  • 4
    • 0020712028 scopus 로고
    • Evidence for an enzyme which cleaves the guanidinobenzoate moiety from active-site titrants specifically designed to inhibit and quantify trypsin
    • Steven, F. S., and Al-Ahmad, R. K. Evidence for an enzyme which cleaves the guanidinobenzoate moiety from active-site titrants specifically designed to inhibit and quantify trypsin. Eur. J. Biochem., 130:335-339,1983.
    • (1983) Eur. J. Biochem. , vol.130 , pp. 335-339
    • Steven, F.S.1    Al-Ahmad, R.K.2
  • 5
    • 33644864110 scopus 로고
    • p'-Guanidinobenzoates: a new active site titrant for trypsin
    • Chase, T., and Shaw, E. p'-Guanidinobenzoates: a new active site titrant for trypsin. Biochem. Biophys. Res. Commun., 29:508-514,1967.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 508-514
    • Chase, T.1    Shaw, E.2
  • 6
    • 0022426117 scopus 로고
    • The design of fluorescent probes which bind to the active centre of guanidinobenzoatase
    • Steven, F. S., Griffin, M. M., and Al-Ahmad, R. K. The design of fluorescent probes which bind to the active centre of guanidinobenzoatase. Eur. J. Biochem., 149:35-40,1985.
    • (1985) Eur. J. Biochem. , vol.149 , pp. 35-40
    • Steven, F.S.1    Griffin, M.M.2    Al-Ahmad, R.K.3
  • 7
    • 0025366575 scopus 로고
    • Direct evidence for the cell surface location of a protease-inhibitor complex on intact leukaemia cells
    • Steven, F. S., and Griffin, M. M. Direct evidence for the cell surface location of a protease-inhibitor complex on intact leukaemia cells. J. Enzyme Inhibition, 3:311-316,1990.
    • (1990) J. Enzyme Inhibition , vol.3 , pp. 311-316
    • Steven, F.S.1    Griffin, M.M.2
  • 8
    • 1842379968 scopus 로고
    • Inhibition of guanidinobenzoatase: evidence for multiple forms of this protease on different tumour cells
    • Steven, F. S., Griffin, M. M., Freemont, A. J., and Johnson, J. Inhibition of guanidinobenzoatase: evidence for multiple forms of this protease on different tumour cells. J. Enzyme Inhibition, 2: 117-127, 1988.
    • (1988) J. Enzyme Inhibition , vol.2 , pp. 117-127
    • Steven, F.S.1    Griffin, M.M.2    Freemont, A.J.3    Johnson, J.4
  • 9
    • 0023006275 scopus 로고
    • Evidence for inhibitors of the cell surface protease guanidinobenzoatase
    • Steven, F. S., Griffin, M. M., Wong, T. L. H., and Itzhaki, S. Evidence for inhibitors of the cell surface protease guanidinobenzoatase. J. Enzyme Inhibition, 1:127-137, 1986.
    • (1986) J. Enzyme Inhibition , vol.1 , pp. 127-137
    • Steven, F.S.1    Griffin, M.M.2    Wong, T.L.H.3    Itzhaki, S.4
  • 10
    • 0023103688 scopus 로고
    • Tissue type plasminogen activator and urokinase: differences in the reaction pattern with the active-site titrant 4-methy-lumbelliferyl-p-guanidinobenzoate hydrochloride
    • Geiger, M., and Binder, B. R. Tissue type plasminogen activator and urokinase: differences in the reaction pattern with the active-site titrant 4-methy-lumbelliferyl-p-guanidinobenzoate hydrochloride. Biochim. Biophys. Acta, 912:34-40,1987.
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 34-40
    • Geiger, M.1    Binder, B.R.2
  • 11
    • 85034620356 scopus 로고
    • An efficient method for the isolation and separation of basolateral-membrane and luminal-membrane vesicles from rabbit kidney cortex
    • Sheikh, M. I., Kagh-Hansen, U., Jorgensen, K. E., and Roigaard-Petersen, H. An efficient method for the isolation and separation of basolateral-membrane and luminal-membrane vesicles from rabbit kidney cortex. Biochem. J., 208:276-282, 1982.
    • (1982) Biochem. J. , vol.208 , pp. 276-282
    • Sheikh, M.I.1    Kagh-Hansen, U.2    Jorgensen, K.E.3    Roigaard-Petersen, H.4
  • 12
    • 0021424883 scopus 로고
    • Solubilization and reconstitution of membrane proteins of Escherichia coli using alkanoyl-Af-methylglucamides
    • Hanatani, M., Nishifuji, K., Futai, M., and Tsuchiya, T. Solubilization and reconstitution of membrane proteins of Escherichia coli using alkanoyl-Af-methylglucamides. J. Biochem., 95:1349-1353,1984.
    • (1984) J. Biochem. , vol.95 , pp. 1349-1353
    • Hanatani, M.1    Nishifuji, K.2    Futai, M.3    Tsuchiya, T.4
  • 14
    • 0014517882 scopus 로고
    • Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters
    • Chase, T., Jr., and Shaw, E. Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters. Titration of the enzymes. Biochemistry, 8:2212-2224, 1969.
    • (1969) Titration of the enzymes. Biochemistry , vol.8 , pp. 2212-2224
    • Chase, T.1    Shaw, E.2
  • 15
    • 0019874180 scopus 로고
    • Na*-stimulated ATPase activities in kidney basal-lateral plasma membranes
    • Proverbio, F., and Del Castillo, J. R., Na*-stimulated ATPase activities in kidney basal-lateral plasma membranes. Biochim. Biophys. Acta, 646: 99-108,1981.
    • (1981) Biochim. Biophys. Acta , vol.646 , pp. 99-108
    • Proverbio, F.1    Del Castillo, J.R.2
  • 16
    • 0014612161 scopus 로고
    • Thermophilic aminopeptidases from Bacillus stearothermopohilus. I. Isolation, specificity and general properties of the thermostable aminopeptidase
    • Roncari, G., and Zuber, H. Thermophilic aminopeptidases from Bacillus stearothermopohilus. I. Isolation, specificity and general properties of the thermostable aminopeptidase. Int. J. Protein Res., 1:45-61,1969.
    • (1969) Int. J. Protein Res. , vol.1 , pp. 45-61
    • Roncari, G.1    Zuber, H.2
  • 17
    • 78651001645 scopus 로고
    • A microspectrometric method for the determination of cytochrome oxidase
    • Cooperstein, S. J., and Lazarow, A. A microspectrometric method for the determination of cytochrome oxidase. J. Biol. Chem., 189:665-670,1951.
    • (1951) J. Biol. Chem. , vol.189 , pp. 665-670
    • Cooperstein, S.J.1    Lazarow, A.2
  • 18
    • 84988106922 scopus 로고
    • Enzyme-structure relationships in the endoplasmic reticulum of rat liver
    • Ernster, L., Siekevitz, P., and Palade, G. E. Enzyme-structure relationships in the endoplasmic reticulum of rat liver. J. CeU. Biol., 15:541-562,1982.
    • (1982) J. CeU. Biol. , vol.15 , pp. 541-562
    • Ernster, L.1    Siekevitz, P.2    Palade, G.E.3
  • 19
    • 78651047890 scopus 로고
    • Comparative study of the binding of acid phosphatase, b-glucuronidase and cathepsin by rat liver particles
    • Gianetto, R., and De Duve, C. Comparative study of the binding of acid phosphatase, b-glucuronidase and cathepsin by rat liver particles. Biochem. J., 59:433-438,1955.
    • (1955) Biochem. J. , vol.59 , pp. 433-438
    • Gianetto, R.1    De Duve, C.2
  • 20
    • 84970068811 scopus 로고
    • Trypsinogens and trypsins of various species
    • Walsh, K. A. Trypsinogens and trypsins of various species. Methods En-zymol., 45:40-63, 1976.
    • (1976) Methods En-zymol. , vol.45 , pp. 40-63
    • Walsh, K.A.1
  • 21
    • 77955296886 scopus 로고
    • Human plasminogen and plasmin
    • Robbins, K. C., and Summaria, L. Human plasminogen and plasmin. Methods Enzymol., 19:184-190,1970.
    • (1970) Methods Enzymol. , vol.19 , pp. 184-190
    • Robbins, K.C.1    Summaria, L.2
  • 22
    • 0016552978 scopus 로고
    • Specific spectrophotometric assays for cathepsin B
    • Bajkowski, A. S., and Franfater, A. Specific spectrophotometric assays for cathepsin B. Anal. Biochem., 68:119-127,1975.
    • (1975) Anal. Biochem. , vol.68 , pp. 119-127
    • Bajkowski, A.S.1    Franfater, A.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature (Lond.), 227:680-685, 1970.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0016711037 scopus 로고
    • High resolution two dimensional electrophoresis of proteins
    • O'Farrell, P. High resolution two dimensional electrophoresis of proteins. J. Biol. Chem., 250:4007-4021,1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 4007-4021
    • O'Farrell, P.1
  • 25
    • 0019492995 scopus 로고
    • Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins
    • Merril, C. R., Goldman, D., Sedman, S. A., and Ebert, M. H. Ultrasensitive stain for proteins in polyacrylamide gels shows regional variations in cerebrospinal fluid proteins. Science (Washington DC), 211:1437-1439,1981.
    • (1981) Science (Washington DC) , vol.211 , pp. 1437-1439
    • Merril, C.R.1    Goldman, D.2    Sedman, S.A.3    Ebert, M.H.4
  • 26
    • 0023646314 scopus 로고
    • Amiloride selectively inhibits the urokinase-type plasminogen activator
    • Vassalli, J. D., and Belin, D. Amiloride selectively inhibits the urokinase-type plasminogen activator. FEBS Lett., 214:187-191,1987.
    • (1987) FEBS Lett. , vol.214 , pp. 187-191
    • Vassalli, J.D.1    Belin, D.2
  • 27
    • 0023139217 scopus 로고
    • Differential reactivity of Dansyl-Glu-Gly-Arg-CH2-Cl, a synthetic urokinase inhibitor, with single-chain and two-chain forms of urokinase-type plasminogen activator
    • Lynen, H. R., Van Hoef, B., and Collen, D. Differential reactivity of Dansyl-Glu-Gly-Arg-CH2-Cl, a synthetic urokinase inhibitor, with single-chain and two-chain forms of urokinase-type plasminogen activator. Eur. J. Biochem., 162:351-356,1987.
    • (1987) Eur. J. Biochem. , vol.162 , pp. 351-356
    • Lynen, H.R.1    Van Hoef, B.2    Collen, D.3
  • 28
    • 0019888627 scopus 로고
    • Tryptase from human pulmonary mast cells
    • Schwartz, L. B., Lewis, R. A., and Austen, K. F. Tryptase from human pulmonary mast cells. J. Biol. Chem., 256:11939-11943,1983.
    • (1983) J. Biol. Chem. , vol.256 , pp. 11939-11943
    • Schwartz, L.B.1    Lewis, R.A.2    Austen, K.F.3
  • 29
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoshlahti, E., and Piersbacher, M. D. New perspectives in cell adhesion: RGD and integrins. Science (Washington DC), 238:491-497, 1987.
    • (1987) Science (Washington DC) , vol.238 , pp. 491-497
    • Ruoshlahti, E.1    Piersbacher, M.D.2
  • 30
    • 0025287207 scopus 로고
    • The targeting of agmatine-liganded mitomycin C to an enzyme on the surface of tumour cells
    • Steven, F. S., Griffin, M. M., and Talbot, I. C. The targeting of agmatine-liganded mitomycin C to an enzyme on the surface of tumour cells. Anticancer Res., 10: 583-590,1990
    • (1990) Anticancer Res. , vol.10 , pp. 583-590
    • Steven, F.S.1    Griffin, M.M.2    Talbot, I.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.