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Volumn 1344, Issue 1, 1997, Pages 6-37

Covalent inhibition of digestive lipases: An in vitro study

Author keywords

[No Author keywords available]

Indexed keywords

AJOENE; BORONIC ACID DERIVATIVE; FENFLURAMINE; IODINE; PARAOXON; PHOSPHONIC ACID DERIVATIVE; TRIACYLGLYCEROL LIPASE;

EID: 0031556926     PISSN: 00052760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2760(97)81102-2     Document Type: Review
Times cited : (74)

References (131)
  • 1
    • 0024806806 scopus 로고
    • Gastric lipases: Biochemical and physiological studies.
    • Gargouri, Y., Moreau, H. and Verger, R. (1989) Gastric lipases: Biochemical and physiological studies. Biochim. Biophys. Acta 1006, 255-271.
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 255-271
    • Gargouri, Y.1    Moreau, H.2    Verger, R.3
  • 4
    • 0027250231 scopus 로고
    • Secretion and contribution to lipolysis of gastric and pancreatic lipases during a test meal in humans.
    • Carrière, F., Barrowman, J.A., Verger, R. and Laugier, R. (1993) Secretion and contribution to lipolysis of gastric and pancreatic lipases during a test meal in humans. Gastroenterology 105, 876-888.
    • (1993) Gastroenterology , vol.105 , pp. 876-888
    • Carrière, F.1    Barrowman, J.A.2    Verger, R.3    Laugier, R.4
  • 6
    • 0024548560 scopus 로고
    • Fatty acids generated by gastric lipase promote human milk triacylglycerol digestion by pancreatic colipase-dependent lipase.
    • Bernbäck, S., Bläckberg, L. and Hernell, O. (1989) Fatty acids generated by gastric lipase promote human milk triacylglycerol digestion by pancreatic colipase-dependent lipase. Biochim. Biophys. Acta 1001, 286-291.
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 286-291
    • Bernbäck, S.1    Bläckberg, L.2    Hernell, O.3
  • 7
    • 0023611098 scopus 로고
    • Dietary treatments of obesity.
    • Bennet, W. (1987) Dietary treatments of obesity. Ann. N. Y. Acad. Sci. 449, 250-263.
    • (1987) Ann. N. Y. Acad. Sci. , vol.449 , pp. 250-263
    • Bennet, W.1
  • 9
    • 0025062291 scopus 로고
    • Structure of human pancreatic lipase.
    • Winkler, F.K., d'Arcy, A. and Hunziker, W. (1990) Structure of human pancreatic lipase. Nature 343, 771-774.
    • (1990) Nature , vol.343 , pp. 771-774
    • Winkler, F.K.1    D'Arcy, A.2    Hunziker, W.3
  • 11
    • 0024593130 scopus 로고
    • Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase.
    • Persson, B., Bentsson-Olivecrona, G., Enerbäck, S., Olivecrona, T. and Jörnvall, H. (1989) Structural features of lipoprotein lipase. Lipase family relationships, binding interactions, non-equivalence of lipase cofactors, vitellogenin similarities and functional subdivision of lipoprotein lipase. Eur. J. Biochem. 179, 39-45.
    • (1989) Eur. J. Biochem. , vol.179 , pp. 39-45
    • Persson, B.1    Bentsson-Olivecrona, G.2    Enerbäck, S.3    Olivecrona, T.4    Jörnvall, H.5
  • 12
    • 0026355156 scopus 로고
    • Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase.
    • Derewenda, Z.S. and Cambillau, C. (1991) Effects of gene mutations in lipoprotein and hepatic lipases as interpreted by a molecular model of the pancreatic triglyceride lipase. J. Biol. Chem. 266, 23112-23119.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23112-23119
    • Derewenda, Z.S.1    Cambillau, C.2
  • 13
    • 0026572737 scopus 로고
    • Structure and evolution of the lipase superfamily.
    • Hide, W.A., Chan, L. and Li, W.H. (1992) Structure and evolution of the lipase superfamily. J. Lipid Res. 33, 167-178.
    • (1992) J. Lipid Res. , vol.33 , pp. 167-178
    • Hide, W.A.1    Chan, L.2    Li, W.H.3
  • 14
    • 0028129833 scopus 로고
    • Lipoprotein lipase. Molecular model based on the pancreatic lipase X-Ray structure: consequences for heparin binding and catalysis.
    • Van Tilbeurgh, H., Roussel, A., Lalouel, J.M. and Cambillau, C. (1994) Lipoprotein lipase. Molecular model based on the pancreatic lipase X-Ray structure: consequences for heparin binding and catalysis. J. Biol. Chem. 269, 4626-4633.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4626-4633
    • Van Tilbeurgh, H.1    Roussel, A.2    Lalouel, J.M.3    Cambillau, C.4
  • 17
    • 0026418190 scopus 로고
    • Lipases reach the surface.
    • Blow, D. (1991) Lipases reach the surface. Nature 351, 444-445.
    • (1991) Nature , vol.351 , pp. 444-445
    • Blow, D.1
  • 18
    • 0026305078 scopus 로고
    • Relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases.
    • Derewenda, Z.S. and Derewenda, U. (1991) Relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases. Biochem. Cell Biol. 69, 842-851.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 842-851
    • Derewenda, Z.S.1    Derewenda, U.2
  • 19
    • 0026786234 scopus 로고
    • The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution.
    • Derewenda, Z.S., Derewenda, U. and Dodson, G.G. (1992) The crystal and molecular structure of the Rhizomucor miehei triacylglyceride lipase at 1.9 Å resolution. J. Mol. Biol. 227, 818-839.
    • (1992) J. Mol. Biol. , vol.227 , pp. 818-839
    • Derewenda, Z.S.1    Derewenda, U.2    Dodson, G.G.3
  • 22
    • 0019887425 scopus 로고
    • Characterization of the serine reacting with diethyl p-nitrophenylphosphate in porcine pancreatic lipase.
    • Guidoni, A., Benkouka, F., de Caro, J. and Rovery, M. (1981) Characterization of the serine reacting with diethyl p-nitrophenylphosphate in porcine pancreatic lipase. Biochim. Biophys. Acta 660, 148-150.
    • (1981) Biochim. Biophys. Acta , vol.660 , pp. 148-150
    • Guidoni, A.1    Benkouka, F.2    De Caro, J.3    Rovery, M.4
  • 23
    • 0017114559 scopus 로고
    • Mechanism of pancreatic lipase action. 1. Interfacial activation of pancreatic lipase.
    • Chapus, C., Sémériva, M., Bovier-Lapierre, C. and Desnuelle, P. (1976) Mechanism of pancreatic lipase action. 1. Interfacial activation of pancreatic lipase. Biochemistry 15, 4980-4987.
    • (1976) Biochemistry , vol.15 , pp. 4980-4987
    • Chapus, C.1    Sémériva, M.2    Bovier-Lapierre, C.3    Desnuelle, P.4
  • 24
    • 0026590627 scopus 로고
    • Large spectral changes accompany the conformational transition of human pancreatic lipase induced by acylation with the inhibitor tetrahydrolipstatin.
    • Lüthi-Peng, Q. and Winkler, F.K. (1992) Large spectral changes accompany the conformational transition of human pancreatic lipase induced by acylation with the inhibitor tetrahydrolipstatin. Eur. J. Biochem. 205, 383-390.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 383-390
    • Lüthi-Peng, Q.1    Winkler, F.K.2
  • 25
    • 0027200087 scopus 로고
    • Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-Ray crystallography.
    • Van Tilbeurgh, H., Egloff, M.-P., Martinez, C., Rugani, N., Verger, R. and Cambillau, C. (1993) Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-Ray crystallography. Nature 362, 814-820.
    • (1993) Nature , vol.362 , pp. 814-820
    • Van Tilbeurgh, H.1    Egloff, M.-P.2    Martinez, C.3    Rugani, N.4    Verger, R.5    Cambillau, C.6
  • 26
    • 0030928763 scopus 로고    scopus 로고
    • A critical re-evaluation of the phenomenon of `interfacial activation'.
    • in press.
    • Ferrato, F., Carrière, F., Sarda, L. and Verger, R. (1997) A critical re-evaluation of the phenomenon of `interfacial activation'. Methods Enzymol., in press.
    • (1997) Methods Enzymol.
    • Ferrato, F.1    Carrière, F.2    Sarda, L.3    Verger, R.4
  • 27
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-procolipase complex.
    • van Tilbeurgh, H., Sarda, L., Verger, R. and Cambillau, C. (1992) Structure of the pancreatic lipase-procolipase complex. Nature 359, 159-162.
    • (1992) Nature , vol.359 , pp. 159-162
    • Van Tilbeurgh, H.1    Sarda, L.2    Verger, R.3    Cambillau, C.4
  • 28
    • 0028308705 scopus 로고
    • Horse pancreatic lipase - the crystal structure refined at 2 center dot 3 ångström resolution.
    • Bourne, Y., Martinez, C., Kerfelec, B., Lombardo, D., Chapus, C. and Cambillau, C. (1994) Horse pancreatic lipase - the crystal structure refined at 2 center dot 3 ångström resolution. J. Mol. Biol. 238, 709-732.
    • (1994) J. Mol. Biol. , vol.238 , pp. 709-732
    • Bourne, Y.1    Martinez, C.2    Kerfelec, B.3    Lombardo, D.4    Chapus, C.5    Cambillau, C.6
  • 29
    • 0024339379 scopus 로고
    • Interface-mediated inactivation of pancreatic lipase by a water-reactive compound: 2-sulfobenzoic cyclic anhydride.
    • Moulin, A., Fourneron, J.-D., Piéroni, G. and Verger, R. (1989) Interface-mediated inactivation of pancreatic lipase by a water-reactive compound: 2-sulfobenzoic cyclic anhydride. Biochemistry 28, 6340-6346.
    • (1989) Biochemistry , vol.28 , pp. 6340-6346
    • Moulin, A.1    Fourneron, J.-D.2    Piéroni, G.3    Verger, R.4
  • 31
    • 0027738967 scopus 로고
    • Inactivation of pancreatic lipases by amphiphilic reagents 5-(Dodecyldithio)-2-nitrobenzoic acid and tetrahydrolipstatin. Dependence upon partitioning between micellar and oil phases.
    • Cudrey, C., Van Tilbeurgh, H., Gargouri, Y. and Verger, R. (1993) Inactivation of pancreatic lipases by amphiphilic reagents 5-(Dodecyldithio)-2-nitrobenzoic acid and tetrahydrolipstatin. Dependence upon partitioning between micellar and oil phases. Biochemistry 32, 13800-13808.
    • (1993) Biochemistry , vol.32 , pp. 13800-13808
    • Cudrey, C.1    Van Tilbeurgh, H.2    Gargouri, Y.3    Verger, R.4
  • 32
    • 0015877388 scopus 로고
    • Action of phospholipase A at interfaces.
    • Verger, R., Mieras, M.C.E. and De Haas, G.H. (1973) Action of phospholipase A at interfaces. J. Biol. Chem. 248, 4023-4034.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4023-4034
    • Verger, R.1    Mieras, M.C.E.2    De Haas, G.H.3
  • 33
    • 0025064233 scopus 로고
    • Competitive inhibition of lipolytic enzymes. I. A kinetic model applicable to water-insoluble competitive inhibitors.
    • Ransac, S., Rivière, C., Gancet, C., Verger, R. and de Haas, G.H. (1990) Competitive inhibition of lipolytic enzymes. I. A kinetic model applicable to water-insoluble competitive inhibitors. Biochim. Biophys. Acta 1043, 57-66.
    • (1990) Biochim. Biophys. Acta , vol.1043 , pp. 57-66
    • Ransac, S.1    Rivière, C.2    Gancet, C.3    Verger, R.4    De Haas, G.H.5
  • 34
    • 0026039544 scopus 로고
    • Inactivation of pancreatic and gastric lipases by tetrahydrolipstatin and alkyl-dithio-5-(2-nitrobenzoic acid).
    • A kinetic study with 1,2-didecanoyl-sn-glycerol monolayers.
    • Ransac, S., Gargouri, Y., Moreau, H. and Verger, R. (1991) Inactivation of pancreatic and gastric lipases by tetrahydrolipstatin and alkyl-dithio-5-(2-nitrobenzoic acid). A kinetic study with 1,2-didecanoyl-sn-glycerol monolayers. Eur. J. Biochem. 202, 395-400.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 395-400
    • Ransac, S.1    Gargouri, Y.2    Moreau, H.3    Verger, R.4
  • 39
  • 40
    • 0014986678 scopus 로고
    • Méthode d'étude des réactions enzymatiques sur une interface.
    • Dervichian, D.G. (1971) Méthode d'étude des réactions enzymatiques sur une interface. Biochimie 53, 25-34.
    • (1971) Biochimie , vol.53 , pp. 25-34
    • Dervichian, D.G.1
  • 41
    • 0015184528 scopus 로고
    • Kinetic analysis of the hydrolysis of lecithin monolayers by phospholipase A.
    • Zografi, G., Verger, R. and De Haas, G.H. (1971) Kinetic analysis of the hydrolysis of lecithin monolayers by phospholipase A. Chem. Phys. Lipids 7, 185-206.
    • (1971) Chem. Phys. Lipids , vol.7 , pp. 185-206
    • Zografi, G.1    Verger, R.2    De Haas, G.H.3
  • 42
    • 0018801496 scopus 로고
    • Hydrolysis of mixed monomolecular films of triglyceride/lecithin by pancreatic lipase.
    • Piéroni, G. and Verger, R. (1979) Hydrolysis of mixed monomolecular films of triglyceride/lecithin by pancreatic lipase. J. Biol. Chem. 254, 10090-10094.
    • (1979) J. Biol. Chem. , vol.254 , pp. 10090-10094
    • Piéroni, G.1    Verger, R.2
  • 43
    • 0014458576 scopus 로고
    • Purification from porcine pancreas of two molecular species with lipase activity.
    • Verger, R., de Haas, G.H., Sarda, L. and Desnuelle, P. (1969) Purification from porcine pancreas of two molecular species with lipase activity. Biochim. Biophys. Acta 188, 272-282.
    • (1969) Biochim. Biophys. Acta , vol.188 , pp. 272-282
    • Verger, R.1    De Haas, G.H.2    Sarda, L.3    Desnuelle, P.4
  • 44
    • 0015504876 scopus 로고
    • Action of organophosphate and sulfonyl halides on porcine pancreatic lipase.
    • Maylié, M.F., Charles, M. and Desnuelle, P. (1972) Action of organophosphate and sulfonyl halides on porcine pancreatic lipase. Biochim. Biophys. Acta 276, 162-175.
    • (1972) Biochim. Biophys. Acta , vol.276 , pp. 162-175
    • Maylié, M.F.1    Charles, M.2    Desnuelle, P.3
  • 45
    • 0011376989 scopus 로고
    • Contribution à l'étude de la lipase pancréatique de porc.
    • Marseille, France.
    • Verger, R. (1970) Contribution à l'étude de la lipase pancréatique de porc. Thesis, Faculté des Sciences de Marseille, Marseille, France.
    • (1970) Thesis, Faculté des Sciences de Marseille
    • Verger, R.1
  • 46
    • 0001097711 scopus 로고
    • Inhibition de la lipase pancréatique par le diéthyl-p-nitrophényl phosphate en émulsion.
    • Desnuelle, P., Sarda, L. and Ailhaud, G. (1960) Inhibition de la lipase pancréatique par le diéthyl-p-nitrophényl phosphate en émulsion. Biochim. Biophys. Acta 37, 570-571.
    • (1960) Biochim. Biophys. Acta , vol.37 , pp. 570-571
    • Desnuelle, P.1    Sarda, L.2    Ailhaud, G.3
  • 47
    • 0018128334 scopus 로고
    • Inhibition of pancreatic lipase by mixed micelles of diethyl p-nitrophenyl phosphate and the bile salts.
    • Rouard, M., Sari, H., Nurit, S., Entressangles, B. and Desnuelle, P. (1978) Inhibition of pancreatic lipase by mixed micelles of diethyl p-nitrophenyl phosphate and the bile salts. Biochim. Biophys. Acta 530, 227-235.
    • (1978) Biochim. Biophys. Acta , vol.530 , pp. 227-235
    • Rouard, M.1    Sari, H.2    Nurit, S.3    Entressangles, B.4    Desnuelle, P.5
  • 48
    • 0017166097 scopus 로고
    • Mechanism of pancreatic lipase action. 2. Catalytic properties of modified lipases.
    • Chapus, C. and Sémériva, M. (1976) Mechanism of pancreatic lipase action. 2. Catalytic properties of modified lipases. Biochemistry 15, 4988-4991.
    • (1976) Biochemistry , vol.15 , pp. 4988-4991
    • Chapus, C.1    Sémériva, M.2
  • 50
    • 0026432669 scopus 로고
    • Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum.
    • Schrag, J.D., Li, Y., Wu, S. and Cygler, M. (1991) Ser-His-Glu triad forms the catalytic site of the lipase from Geotrichum candidum. Nature 351, 761-764.
    • (1991) Nature , vol.351 , pp. 761-764
    • Schrag, J.D.1    Li, Y.2    Wu, S.3    Cygler, M.4
  • 51
    • 0026583770 scopus 로고
    • Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.
    • Martinez, C., de Geus, P., Lauwereys, M., Matthyssens, G. and Cambillau, C. (1992) Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent. Nature 356, 615-618.
    • (1992) Nature , vol.356 , pp. 615-618
    • Martinez, C.1    De Geus, P.2    Lauwereys, M.3    Matthyssens, G.4    Cambillau, C.5
  • 53
    • 0027435346 scopus 로고
    • The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.
    • Noble, M.E.M., Cleasby, A., Johnson, L.N., Egmond, M.R. and Frenken, L.G.J. (1993) The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate. FEBS Lett. 331, 123-128.
    • (1993) FEBS Lett. , vol.331 , pp. 123-128
    • Noble, M.E.M.1    Cleasby, A.2    Johnson, L.N.3    Egmond, M.R.4    Frenken, L.G.J.5
  • 55
    • 0028280556 scopus 로고
    • Probing the nature of substrate binding in Humicola lanuginosa lipase through X-ray crystallography and intuitive modelling.
    • Lawson, D.M., Brzozowski, A.M., Rety, S., Verma, C. and Dodson, G.G. (1994) Probing the nature of substrate binding in Humicola lanuginosa lipase through X-ray crystallography and intuitive modelling. Protein Eng. 7, 543-550.
    • (1994) Protein Eng. , vol.7 , pp. 543-550
    • Lawson, D.M.1    Brzozowski, A.M.2    Rety, S.3    Verma, C.4    Dodson, G.G.5
  • 56
    • 0028773288 scopus 로고
    • Sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica.
    • Uppenberg, J., Hansen, M.T., Patkar, S. and Jones, T.A. (1994) Sequence, crystal structure determination and refinement of two crystal forms of lipase B from Candida antarctica. Structure 2, 293-308.
    • (1994) Structure , vol.2 , pp. 293-308
    • Uppenberg, J.1    Hansen, M.T.2    Patkar, S.3    Jones, T.A.4
  • 57
    • 0020452215 scopus 로고
    • Purification and properties of an acid lipase from human gastric juice.
    • Tiruppathi, C. and Balasubramanian, K.A. (1982) Purification and properties of an acid lipase from human gastric juice. Biochim. Biophys. Acta 712, 692-697.
    • (1982) Biochim. Biophys. Acta , vol.712 , pp. 692-697
    • Tiruppathi, C.1    Balasubramanian, K.A.2
  • 58
    • 0023927028 scopus 로고
    • Purification, characterization and kinetic properties of the rabbit gastric lipase.
    • Moreau, H., Gargouri, Y., Lecat, D., Junien, J.-L. and Verger, R. (1988) Purification, characterization and kinetic properties of the rabbit gastric lipase. Biochim. Biophys. Acta 960, 286-293.
    • (1988) Biochim. Biophys. Acta , vol.960 , pp. 286-293
    • Moreau, H.1    Gargouri, Y.2    Lecat, D.3    Junien, J.-L.4    Verger, R.5
  • 59
    • 0026093529 scopus 로고
    • Inactivation of gastric and pancreatic lipases by diethyl p-nitrophenyl phosphate.
    • Moreau, H., Moulin, A., Gargouri, Y., Noël, J.-P. and Verger, R. (1991) Inactivation of gastric and pancreatic lipases by diethyl p-nitrophenyl phosphate. Biochemistry 30, 1037-1041.
    • (1991) Biochemistry , vol.30 , pp. 1037-1041
    • Moreau, H.1    Moulin, A.2    Gargouri, Y.3    Noël, J.-P.4    Verger, R.5
  • 61
    • 0023789808 scopus 로고
    • Importance of sulfhydryl group for rabbit gastric lipase activity.
    • Moreau, H., Gargouri, Y., Piéroni, G. and Verger, R. (1988) Importance of sulfhydryl group for rabbit gastric lipase activity. FEBS Lett. 236, 383-387.
    • (1988) FEBS Lett. , vol.236 , pp. 383-387
    • Moreau, H.1    Gargouri, Y.2    Piéroni, G.3    Verger, R.4
  • 62
    • 0026802491 scopus 로고
    • The catalytic site residues and interfacial binding of human pancreatic lipase.
    • Lowe, M.E. (1992) The catalytic site residues and interfacial binding of human pancreatic lipase. J. Biol. Chem. 267, 17069-17073.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17069-17073
    • Lowe, M.E.1
  • 63
    • 0021802672 scopus 로고
    • Limited proteolysis of porcine pancreatic lipase.
    • Bousset-Risso, M., Bonicel, J. and Rovery, M. (1985) Limited proteolysis of porcine pancreatic lipase. FEBS Lett. 182, 323-326.
    • (1985) FEBS Lett. , vol.182 , pp. 323-326
    • Bousset-Risso, M.1    Bonicel, J.2    Rovery, M.3
  • 64
    • 0022476228 scopus 로고
    • Hydrolysis of p-nitrophenyl acetate by the peptide chain fragment (336-449) of porcine pancreatic lipase.
    • de Caro, J.D., Rouimi, P. and Rovery, M. (1986) Hydrolysis of p-nitrophenyl acetate by the peptide chain fragment (336-449) of porcine pancreatic lipase. Eur. J. Biochem. 158, 601-607.
    • (1986) Eur. J. Biochem. , vol.158 , pp. 601-607
    • De Caro, J.D.1    Rouimi, P.2    Rovery, M.3
  • 65
    • 0026503261 scopus 로고
    • Sequence of horse pancreatic lipase as determined by protein and cDNA sequencing.
    • Implications for p-nitrophenyl acetate hydrolysis by pancreatic lipases.
    • Kerfelec, B., Foglizzo, E., Bonicel, J., Bougis, P.E. and Chapus, C. (1992) Sequence of horse pancreatic lipase as determined by protein and cDNA sequencing. Implications for p-nitrophenyl acetate hydrolysis by pancreatic lipases. Eur. J. Biochem. 206, 279-287.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 279-287
    • Kerfelec, B.1    Foglizzo, E.2    Bonicel, J.3    Bougis, P.E.4    Chapus, C.5
  • 71
    • 0028889185 scopus 로고
    • Stereoselectivity of microbial lipases.
    • The substitution at position sn-2 of triacylglycerol analogs influences the stereoselectivity of different microbial lipases.
    • Stadler, P., Kovac, A., Haalck, L., Spener, F. and Paltauf, F. (1995) Stereoselectivity of microbial lipases. The substitution at position sn-2 of triacylglycerol analogs influences the stereoselectivity of different microbial lipases. Eur. J. Biochem. 227, 335-343.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 335-343
    • Stadler, P.1    Kovac, A.2    Haalck, L.3    Spener, F.4    Paltauf, F.5
  • 72
    • 0011338173 scopus 로고    scopus 로고
    • Molecular or interfacial recognition chirality in the inhibition of digestive lipases by chiral organophosphorus triglycerides analogs?
    • submitted.
    • Marguet, F., Douchet, I., Verger, R. and Buono, G. (1997) Molecular or interfacial recognition chirality in the inhibition of digestive lipases by chiral organophosphorus triglycerides analogs? J. Am. Chem. Soc., submitted.
    • (1997) J. Am. Chem. Soc.
    • Marguet, F.1    Douchet, I.2    Verger, R.3    Buono, G.4
  • 73
    • 0027506517 scopus 로고
    • Stereoselective hydrolysis of triglycerides by animal and microbial lipases.
    • Rogalska, E., Cudrey, C., Ferrato, F. and Verger, R. (1993) Stereoselective hydrolysis of triglycerides by animal and microbial lipases. Chirality 5, 24-30.
    • (1993) Chirality , vol.5 , pp. 24-30
    • Rogalska, E.1    Cudrey, C.2    Ferrato, F.3    Verger, R.4
  • 74
    • 0025202769 scopus 로고
    • Stereoselectivity of lipases. I.
    • Hydrolysis of enantiomeric glyceride analogues by gastric and pancreatic lipases. A kinetic study using the monomolecular film technique.
    • Ransac, S., Rogalska, E., Gargouri, Y., Deveer, A.M.T.J., Paltauf, F., de Haas, G.H. and Verger, R. (1990) Stereoselectivity of lipases. I. Hydrolysis of enantiomeric glyceride analogues by gastric and pancreatic lipases. A kinetic study using the monomolecular film technique. J. Biol. Chem. 265, 20263-20270.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20263-20270
    • Ransac, S.1    Rogalska, E.2    Gargouri, Y.3    Deveer, A.M.T.J.4    Paltauf, F.5    De Haas, G.H.6    Verger, R.7
  • 75
    • 0029586708 scopus 로고
    • Lipase stereoselectivity and regioselectivity toward three isomers of dicaprin: A kinetic study by the monomolecular film technique.
    • Rogalska, E., Nury, S., Douchet, I. and Verger, R. (1995) Lipase stereoselectivity and regioselectivity toward three isomers of dicaprin: A kinetic study by the monomolecular film technique. Chirality 7, 505-515.
    • (1995) Chirality , vol.7 , pp. 505-515
    • Rogalska, E.1    Nury, S.2    Douchet, I.3    Verger, R.4
  • 81
    • 0028103723 scopus 로고
    • Two conformational states of Candida rugosa lipase.
    • Grochulski, P., Li, Y., Schrag, J.D. and Cygler, M. (1994) Two conformational states of Candida rugosa lipase. Protein Sci. 3, 82-91.
    • (1994) Protein Sci. , vol.3 , pp. 82-91
    • Grochulski, P.1    Li, Y.2    Schrag, J.D.3    Cygler, M.4
  • 84
    • 0001449008 scopus 로고
    • Studies on the active site topography of pancreatic lipase with organo-boronic acids as bifunctional reversible inhibitors.
    • Rotanova, T.V., Claus, R., Ivanova, A.G., Ginodman, L. and Antonov, V.K. (1976) Studies on the active site topography of pancreatic lipase with organo-boronic acids as bifunctional reversible inhibitors. Bioorg. Khim. 2, 837-845.
    • (1976) Bioorg. Khim. , vol.2 , pp. 837-845
    • Rotanova, T.V.1    Claus, R.2    Ivanova, A.G.3    Ginodman, L.4    Antonov, V.K.5
  • 85
    • 0018958861 scopus 로고
    • Boronic acid inhibitors of porcine pancreatic lipase.
    • Garner, C.W. (1980) Boronic acid inhibitors of porcine pancreatic lipase. J. Biol. Chem. 255, 5064-5068.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5064-5068
    • Garner, C.W.1
  • 86
    • 0011285873 scopus 로고
    • The relation of metals and SH groups to the activity of pancreatic lipase.
    • Wills, E.D. (1960) The relation of metals and SH groups to the activity of pancreatic lipase. Biochim. Biophys. Acta 40, 481-490.
    • (1960) Biochim. Biophys. Acta , vol.40 , pp. 481-490
    • Wills, E.D.1
  • 87
    • 0019423110 scopus 로고
    • Effect of fenfluramine and related compounds on the pancreatic colipase/lipase system.
    • Borgström, B. and Wollesen, C. (1981) Effect of fenfluramine and related compounds on the pancreatic colipase/lipase system. FEBS Lett. 126, 25-28.
    • (1981) FEBS Lett. , vol.126 , pp. 25-28
    • Borgström, B.1    Wollesen, C.2
  • 88
    • 0011288864 scopus 로고
    • A factor of protein character in rat liver inhibiting lipase activity of rat pancreas.
    • Machovich, R., Csillag, J. and Naray, A. (1970) A factor of protein character in rat liver inhibiting lipase activity of rat pancreas. FEBS Lett. 9, 119-120.
    • (1970) FEBS Lett. , vol.9 , pp. 119-120
    • Machovich, R.1    Csillag, J.2    Naray, A.3
  • 89
    • 0015352799 scopus 로고
    • Isolierung und Charakterisierung eines Lipase Hemmstoffes aus Lipiden von Arachis hypogaea.
    • Hochstrasser, K., Feuth, H. and Werle, E. (1972) Isolierung und Charakterisierung eines Lipase Hemmstoffes aus Lipiden von Arachis hypogaea. Hoppe-Seylers Z. Physiol. Chem. 353, 855-860.
    • (1972) Hoppe-Seylers Z. Physiol. Chem. , vol.353 , pp. 855-860
    • Hochstrasser, K.1    Feuth, H.2    Werle, E.3
  • 90
    • 0015859269 scopus 로고
    • A protein inhibiting pancreatic lipase activity in soybean seeds.
    • Mori, T., Satouchi, K. and Matsushita, S. (1973) A protein inhibiting pancreatic lipase activity in soybean seeds. Agr. Biol. Chem. 37, 1225-1226.
    • (1973) Agr. Biol. Chem. , vol.37 , pp. 1225-1226
    • Mori, T.1    Satouchi, K.2    Matsushita, S.3
  • 91
    • 0021691503 scopus 로고
    • Studies on the inhibition of pancreatic and microbial lipases by soybean proteins.
    • Gargouri, Y., Julien, R., Piéroni, G., Verger, R. and Sarda, L. (1984) Studies on the inhibition of pancreatic and microbial lipases by soybean proteins. J. Lipids Res. 25, 1214-1221.
    • (1984) J. Lipids Res. , vol.25 , pp. 1214-1221
    • Gargouri, Y.1    Julien, R.2    Piéroni, G.3    Verger, R.4    Sarda, L.5
  • 93
    • 0017899750 scopus 로고
    • Interactions of serum albumin and other proteins with pancreatic lipase.
    • Borgström, B. and Erlanson, C. (1978) Interactions of serum albumin and other proteins with pancreatic lipase. Gastroenterology 75, 382-386.
    • (1978) Gastroenterology , vol.75 , pp. 382-386
    • Borgström, B.1    Erlanson, C.2
  • 94
    • 0018545617 scopus 로고
    • Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts.
    • Bläckberg, L., Hernell, O., Bengtsson, G. and Olivecrona, T. (1979) Colipase enhances hydrolysis of dietary triglycerides in the absence of bile salts. J. Clin. Invest. 64, 1303-1308.
    • (1979) J. Clin. Invest. , vol.64 , pp. 1303-1308
    • Bläckberg, L.1    Hernell, O.2    Bengtsson, G.3    Olivecrona, T.4
  • 95
  • 96
    • 0001474412 scopus 로고
    • Purification and characterization of proteinous inhibitor of lipase from wheat flour.
    • Tani, H., Ohishi, H. and Watanabe, K. (1994) Purification and characterization of proteinous inhibitor of lipase from wheat flour. J. Agr. Food Chem. 42, 2382-2385.
    • (1994) J. Agr. Food Chem. , vol.42 , pp. 2382-2385
    • Tani, H.1    Ohishi, H.2    Watanabe, K.3
  • 99
    • 0026553297 scopus 로고
    • Pancreatic colipase.
    • Structural and physiological aspects.
    • Erlanson-Albertsson, C. (1992) Pancreatic colipase. Structural and physiological aspects. Biochim. Biophys. Acta 1125, 1-7.
    • (1992) Biochim. Biophys. Acta , vol.1125 , pp. 1-7
    • Erlanson-Albertsson, C.1
  • 102
    • 0015236575 scopus 로고
    • On the sulfhydryl groups of porcine pancreatic lipase and their possible role in the activity of the enzyme.
    • Verger, R., Sarda, L. and Desnuelle, P. (1971) On the sulfhydryl groups of porcine pancreatic lipase and their possible role in the activity of the enzyme. Biochim. Biophys. Acta 242, 580-592.
    • (1971) Biochim. Biophys. Acta , vol.242 , pp. 580-592
    • Verger, R.1    Sarda, L.2    Desnuelle, P.3
  • 103
    • 0022448659 scopus 로고
    • Inhibition of lipases by proteins: A binding study using dicaprin monolayers.
    • Gargouri, Y., Piéroni, G., Rivière, C., Sarda, L. and Verger, R. (1986) Inhibition of lipases by proteins: A binding study using dicaprin monolayers. Biochemistry 25, 1733-1738.
    • (1986) Biochemistry , vol.25 , pp. 1733-1738
    • Gargouri, Y.1    Piéroni, G.2    Rivière, C.3    Sarda, L.4    Verger, R.5
  • 104
    • 0018890516 scopus 로고
    • Enzyme kinetics of lipolysis.
    • Verger, R. (1980) Enzyme kinetics of lipolysis. Methods Enzymol. 64, 340-392.
    • (1980) Methods Enzymol. , vol.64 , pp. 340-392
    • Verger, R.1
  • 110
    • 0016560173 scopus 로고
    • Studies on the mechanism of fat absorption in congenital isolated lipase deficiency.
    • Muller, D.P.R., McCollum, J.P.K., Tompeter, R.S. and Harries, J.T. (1975) Studies on the mechanism of fat absorption in congenital isolated lipase deficiency. Gut 16, 838.
    • (1975) Gut , vol.16 , pp. 838
    • Muller, D.P.R.1    McCollum, J.P.K.2    Tompeter, R.S.3    Harries, J.T.4
  • 112
    • 0026590938 scopus 로고
    • Inactivation of human pancreatic lipase by 5-dodecyldithio-2- nitrobenzoic acid.
    • Gargouri, Y., Cudrey, C., Mejdoub, H. and Verger, R. (1992) Inactivation of human pancreatic lipase by 5-dodecyldithio-2- nitrobenzoic acid. Eur. J. Biochem. 204, 1063-1067.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 1063-1067
    • Gargouri, Y.1    Cudrey, C.2    Mejdoub, H.3    Verger, R.4
  • 113
    • 0024202729 scopus 로고
    • Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin.
    • Hadvàry, P., Lengsfeld, H. and Wolfer, H. (1988) Inhibition of pancreatic lipase in vitro by the covalent inhibitor tetrahydrolipstatin. Biochem. J. 256, 357-361.
    • (1988) Biochem. J. , vol.256 , pp. 357-361
    • Hadvàry, P.1    Lengsfeld, H.2    Wolfer, H.3
  • 114
    • 0023791240 scopus 로고
    • Mode of action of tetrahydrolipstatin: A derivative of the naturally occuring lipase inhibitor lipstatin.
    • Borgström, B. (1988) Mode of action of tetrahydrolipstatin: A derivative of the naturally occuring lipase inhibitor lipstatin. Biochim. Biophys. Acta 962, 308-316.
    • (1988) Biochim. Biophys. Acta , vol.962 , pp. 308-316
    • Borgström, B.1
  • 115
    • 0025911832 scopus 로고
    • The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase.
    • Hadvàry, P., Sidler, W., Meister, W., Vetter, W. and Wolfer, H. (1991) The lipase inhibitor tetrahydrolipstatin binds covalently to the putative active site serine of pancreatic lipase. J. Biol. Chem. 266, 2021-2027.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2021-2027
    • Hadvàry, P.1    Sidler, W.2    Meister, W.3    Vetter, W.4    Wolfer, H.5
  • 116
    • 0026517225 scopus 로고
    • Identification of the active-site serine in human pancreatic lipase by chemical modification with tetrahydrolipstatin.
    • Lüthi-Peng, Q., Maerki, H.P. and Hadvary, P. (1992) Identification of the active-site serine in human pancreatic lipase by chemical modification with tetrahydrolipstatin. FEBS Lett. 299, 111-115.
    • (1992) FEBS Lett. , vol.299 , pp. 111-115
    • Lüthi-Peng, Q.1    Maerki, H.P.2    Hadvary, P.3
  • 117
    • 0002392833 scopus 로고
    • Pharmacological activity (inhibition of fat absorption) and tolerability in healthy volunteers of tetrahydrolipstatin (THL).
    • A specific lipase inhibitor.
    • Güzelhan, C., Crijns, H.J.M.J., Peeters, P.A.M., Jonkman, J.H.G. and Hartmann, D. (1991) Pharmacological activity (inhibition of fat absorption) and tolerability in healthy volunteers of tetrahydrolipstatin (THL). A specific lipase inhibitor. Int. J. Obes. 15, 29.
    • (1991) Int. J. Obes. , vol.15 , pp. 29
    • Güzelhan, C.1    Crijns, H.J.M.J.2    Peeters, P.A.M.3    Jonkman, J.H.G.4    Hartmann, D.5
  • 118
    • 0002543121 scopus 로고
    • Preclinical profile of the lipase inhibitor tetrahydrolipstatin (Ro 18-0647, THL)
    • a potential drug for the treatment of obesity.
    • Meier, M.K., Blum-Kaelin, D., Bremer, K., Isler, D., Joly, R., Keller-Rupp, P. and Lengsfeld, H. (1991) Preclinical profile of the lipase inhibitor tetrahydrolipstatin (Ro 18-0647, THL), a potential drug for the treatment of obesity. Int. J. Obes. 15, 31.
    • (1991) Int. J. Obes. , vol.15 , pp. 31
    • Meier, M.K.1    Blum-Kaelin, D.2    Bremer, K.3    Isler, D.4    Joly, R.5    Keller-Rupp, P.6    Lengsfeld, H.7
  • 119
    • 0026604775 scopus 로고
    • Initial studies in humans with the novel gastrointestinal lipase inhibitor, Ro 18-0647 (tetrahydrolipstatin).
    • Hauptman, J., Jeunet, F. and Hartmann, D. (1992) Initial studies in humans with the novel gastrointestinal lipase inhibitor, Ro 18-0647 (tetrahydrolipstatin). Am. J. Clin. Nutr. 55, 309S-313S.
    • (1992) Am. J. Clin. Nutr. , vol.55
    • Hauptman, J.1    Jeunet, F.2    Hartmann, D.3
  • 120
    • 0027252448 scopus 로고
    • Lipase inhibition - a novel concept in the treatment of obesity.
    • Drent, M.L. and Van der Veen, E.A. (1993) Lipase inhibition - a novel concept in the treatment of obesity. Int. J. Obes. 17, 241-244.
    • (1993) Int. J. Obes. , vol.17 , pp. 241-244
    • Drent, M.L.1    Van der Veen, E.A.2
  • 121
    • 0028001752 scopus 로고
    • Influence of dietary composition on the inhibition of fat absorption by Orlistat.
    • Güzelhan, C., Odink, J., Jansen-Zuidema, J.J.N. and Hartmann, D. (1994) Influence of dietary composition on the inhibition of fat absorption by Orlistat. J. Int. Med. Res. 22, 255-265.
    • (1994) J. Int. Med. Res. , vol.22 , pp. 255-265
    • Güzelhan, C.1    Odink, J.2    Jansen-Zuidema, J.J.N.3    Hartmann, D.4
  • 122
    • 0028149263 scopus 로고
    • Comparison of the inhibition of dietary fat absorption by full versus divided doses of Orlistat.
    • Hussain, Y., Guzelhan, C., Odink, J., Van der Beek, E.J. and Hartmann, D. (1994) Comparison of the inhibition of dietary fat absorption by full versus divided doses of Orlistat. J. Clin. Pharmacol. 34, 1121-1125.
    • (1994) J. Clin. Pharmacol. , vol.34 , pp. 1121-1125
    • Hussain, Y.1    Guzelhan, C.2    Odink, J.3    Van der Beek, E.J.4    Hartmann, D.5
  • 123
    • 0028103894 scopus 로고
    • Retrospective population-based analysis of the dose-response (fecal fat excretion) relationship of Orlistat in normal and obese volunteers.
    • Zhi, J., Melia, A.T., Guerciolini, R., Chung, J., Kinberg, J., Hauptman, J.B. and Patel, I.H. (1994) Retrospective population-based analysis of the dose-response (fecal fat excretion) relationship of Orlistat in normal and obese volunteers. Clin. Pharmacol. Ther. 56, 82-85.
    • (1994) Clin. Pharmacol. Ther. , vol.56 , pp. 82-85
    • Zhi, J.1    Melia, A.T.2    Guerciolini, R.3    Chung, J.4    Kinberg, J.5    Hauptman, J.B.6    Patel, I.H.7
  • 125
    • 0029066761 scopus 로고
    • Effect of the lipase inhibitor orlistat and of dietary lipid on the absorption of radiolabelled triolein, tri-gamma-linolenin and tripalmitin in mice.
    • Isler, D., Moeglen, C., Gains, N. and Meier, M.K. (1995) Effect of the lipase inhibitor orlistat and of dietary lipid on the absorption of radiolabelled triolein, tri-gamma-linolenin and tripalmitin in mice. Br. J. Nutr. 73, 851-862.
    • (1995) Br. J. Nutr. , vol.73 , pp. 851-862
    • Isler, D.1    Moeglen, C.2    Gains, N.3    Meier, M.K.4
  • 126
    • 0028866609 scopus 로고
    • Review of limited systemic absorption of orlistat, a lipase inhibitor, in healthy human volunteers.
    • Zhi, J.G., Melia, A.T., Eggers, H., Joly, R. and Patel, I.H. (1995) Review of limited systemic absorption of orlistat, a lipase inhibitor, in healthy human volunteers. J. Clin. Pharmacol. 35, 1103-1108.
    • (1995) J. Clin. Pharmacol. , vol.35 , pp. 1103-1108
    • Zhi, J.G.1    Melia, A.T.2    Eggers, H.3    Joly, R.4    Patel, I.H.5
  • 127
    • 0029398377 scopus 로고
    • First clinical studies with Orlistat: A short review.
    • Drent, M.L. and Vanderveen, E.A. (1995) First clinical studies with Orlistat: A short review. Obes. Res. 3, S623-S625.
    • (1995) Obes. Res. , vol.3
    • Drent, M.L.1    Vanderveen, E.A.2
  • 128
    • 0024574116 scopus 로고
    • Role of a sulfhydryl group in gastric lipases.
    • A binding study using the monomolecular-film technique.
    • Gargouri, Y., Moreau, H., Piéroni, G. and Verger, R. (1989) Role of a sulfhydryl group in gastric lipases. A binding study using the monomolecular-film technique. Eur. J. Biochem. 180, 367-371.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 367-371
    • Gargouri, Y.1    Moreau, H.2    Piéroni, G.3    Verger, R.4


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