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Volumn 25, Issue 1, 1997, Pages 15-32

Structure and function of gastro-intestinal lipases

Author keywords

Absorption; Bioavailability; Digestion; Drug delivery; Gastro intestinal tract; Lipolysis; Lipolytic enzymes; Triglycerides

Indexed keywords

ABSORPTION; BIOCHEMISTRY; CRYSTAL STRUCTURE; DRUG INTERACTIONS; EMULSIFICATION; FATTY ACIDS; LIPIDS; PHARMACODYNAMICS;

EID: 0343907176     PISSN: 0169409X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-409X(96)00488-7     Document Type: Review
Times cited : (113)

References (66)
  • 2
    • 0006763502 scopus 로고
    • Triglyceride emulsification by amphipaths in the intestinal lumen during digestion of fat
    • Linthorst, J.M., Clark, S.B. and Holt, P.R. (1977) Triglyceride emulsification by amphipaths in the intestinal lumen during digestion of fat. J. Colloid Interface Sci., 60, 1-10.
    • (1977) J. Colloid Interface Sci. , vol.60 , pp. 1-10
    • Linthorst, J.M.1    Clark, S.B.2    Holt, P.R.3
  • 4
    • 49049139770 scopus 로고
    • The phase behaviour of triolein, cholesterol and lecithin emulsions
    • Miller, K.W. and Small, D.M. (1982) The phase behaviour of triolein, cholesterol and lecithin emulsions. J. Colloid Interface Sci. 89, 446-477.
    • (1982) J. Colloid Interface Sci. , vol.89 , pp. 446-477
    • Miller, K.W.1    Small, D.M.2
  • 5
    • 0023829203 scopus 로고
    • Lingual and gastric lipases; species differences in the origin of prepancreatic digestive lipases and in the localization of gastric lipase
    • de Nigris, S.J., Hamosh, M., Kasbekar, D.K., Lee, T.C. and Hamosh, P. (1988) Lingual and gastric lipases; species differences in the origin of prepancreatic digestive lipases and in the localization of gastric lipase. Biochim. Biophys. Acta 959, 38-45.
    • (1988) Biochim. Biophys. Acta , vol.959 , pp. 38-45
    • De Nigris, S.J.1    Hamosh, M.2    Kasbekar, D.K.3    Lee, T.C.4    Hamosh, P.5
  • 6
    • 0021991487 scopus 로고
    • Purification and molecular characterisation of bovine pregastric lipase
    • Bernback, S., Hernell, O. and Blackberg, L. (1985) Purification and molecular characterisation of bovine pregastric lipase. Eur. J. Biochem. 148, 233-238.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 233-238
    • Bernback, S.1    Hernell, O.2    Blackberg, L.3
  • 7
    • 0021684933 scopus 로고
    • Purification and characterization of pregastric esterase from calf
    • Sweet, B.J., Matthews, L.C. and Richardson, T. (1984) Purification and characterization of pregastric esterase from calf. Arch. Biochem. Biophys. 234, 144-150.
    • (1984) Arch. Biochem. Biophys. , vol.234 , pp. 144-150
    • Sweet, B.J.1    Matthews, L.C.2    Richardson, T.3
  • 8
    • 0021100452 scopus 로고
    • Purification and characterization of rat lingual lipase
    • Field, R.B. and Scow, R.O. (1983) Purification and characterization of rat lingual lipase. J. Biol. Chem. 258, 14 563-14 569.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14563-14569
    • Field, R.B.1    Scow, R.O.2
  • 10
    • 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
  • 11
    • 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 1005, 255-271.
    • (1989) Biochim. Biophys. Acta , vol.1005 , pp. 255-271
    • Gargouri, Y.1    Moreau, H.2    Verger, R.3
  • 15
    • 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
  • 16
    • 0019511505 scopus 로고
    • Studies on fat digestion, absorption and transport in the suckling rat. I. Fatty acid composition and concentrations of major lipid components
    • Fernando-Warnakulasuriya, G.J.P., Staggers, J.E., Frost, S.C. and Wells, M.A. (1981) Studies on fat digestion, absorption and transport in the suckling rat. I. Fatty acid composition and concentrations of major lipid components. J. Lipid Res. 22, 668-674.
    • (1981) J. Lipid Res. , vol.22 , pp. 668-674
    • Fernando-Warnakulasuriya, G.J.P.1    Staggers, J.E.2    Frost, S.C.3    Wells, M.A.4
  • 17
    • 0019405808 scopus 로고
    • Studies on fat digestion, absorption and transport in the suckling rat. II. Triacylglycerols: Molecular species, stereospecific analysis and specificity of hydrolysis by lingual lipase
    • Staggers, J.E., Fernando-Warnakulasuriya, G.J.P. and Wells, M.A. (1981) Studies on fat digestion, absorption and transport in the suckling rat. II. Triacylglycerols: molecular species, stereospecific analysis and specificity of hydrolysis by lingual lipase. J. Lipid Res. 22, 675-679.
    • (1981) J. Lipid Res. , vol.22 , pp. 675-679
    • Staggers, J.E.1    Fernando-Warnakulasuriya, G.J.P.2    Wells, M.A.3
  • 18
    • 0024548560 scopus 로고
    • Fatty acids generated by gastric lipase promote human milk triacylglycerol digestion by pancreatic colipase-dependent lipase
    • Bernback, S., Blackberg, 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, 286-293.
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 286-293
    • Bernback, S.1    Blackberg, L.2    Hernell, O.3
  • 19
    • 0002709258 scopus 로고
    • B. Borstrom and H.L. Brockman (Eds.). Elsevier, Amsterdam
    • Hamosh, M. (1984) In: B. Borstrom and H.L. Brockman (Eds.). Lipases. Elsevier, Amsterdam, pp. 49-81.
    • (1984) Lipases , pp. 49-81
    • Hamosh, M.1
  • 20
    • 0342548721 scopus 로고
    • Emulsification of fat in the intestine of the rat and its relationship to absorption
    • Frazer. A.C., Schulman, J.H. and Stewart, H.C. (1944) Emulsification of fat in the intestine of the rat and its relationship to absorption. J. Physiol. 103, 306-316.
    • (1944) J. Physiol. , vol.103 , pp. 306-316
    • Frazer, A.C.1    Schulman, J.H.2    Stewart, H.C.3
  • 21
    • 0025264030 scopus 로고
    • Physical-chemical behaviour of dietary and biliary lipids during intestinal digestion and absorption. 2. Phase behaviour and aggregation states of luminal lipids during duodenal fat digestion in health adult human beings
    • Hernell, O., Staggers, J.E. and Carey, M.C. (1990) Physical-chemical behaviour of dietary and biliary lipids during intestinal digestion and absorption. 2. Phase behaviour and aggregation states of luminal lipids during duodenal fat digestion in health adult human beings. Biochemistry 29, 2041-2056.
    • (1990) Biochemistry , vol.29 , pp. 2041-2056
    • Hernell, O.1    Staggers, J.E.2    Carey, M.C.3
  • 22
    • 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
  • 23
    • 0025348627 scopus 로고
    • Inhibition of lipolysis by hydrocarbons and fatty alcohols
    • Ferreira, G.C. and Patton, J.S. (1990) Inhibition of lipolysis by hydrocarbons and fatty alcohols. J. Lipid Res. 31, 889-897.
    • (1990) J. Lipid Res. , vol.31 , pp. 889-897
    • Ferreira, G.C.1    Patton, J.S.2
  • 24
    • 0021106012 scopus 로고
    • The production of liquid crystalline product phases by pancreatic lipase in the absence of bile salts: A freeze-fracture study
    • Rigler, M.W. and Patton, J.S. (1983) The production of liquid crystalline product phases by pancreatic lipase in the absence of bile salts: a freeze-fracture study. Biochim. Biophys. Acta 751, 444-454.
    • (1983) Biochim. Biophys. Acta , vol.751 , pp. 444-454
    • Rigler, M.W.1    Patton, J.S.2
  • 25
    • 0017850763 scopus 로고
    • Binding of porcine pancreatic lipase and colipase in the absence of substrate studied by 2-phase partition and affinity chromatography
    • Palton, J.S., Albertsson, P.A., Erlanson, C. and Borstrom, B. (1978) Binding of porcine pancreatic lipase and colipase in the absence of substrate studied by 2-phase partition and affinity chromatography. J. Biol. Chem. 253, 4195-4202.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4195-4202
    • Palton, J.S.1    Albertsson, P.A.2    Erlanson, C.3    Borstrom, B.4
  • 26
    • 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
  • 27
    • 0026532653 scopus 로고
    • Uncoupling of catalysis and colipase binding in pancreatic juice by limited proteolysis
    • Abousalham, A., Chaillan, C., Kerfelec, B., Foglizzo, E. and Chapus, C. (1992) Uncoupling of catalysis and colipase binding in pancreatic juice by limited proteolysis. Protein Eng. 5, 105-111.
    • (1992) Protein Eng. , vol.5 , pp. 105-111
    • Abousalham, A.1    Chaillan, C.2    Kerfelec, B.3    Foglizzo, E.4    Chapus, C.5
  • 28
    • 0029051409 scopus 로고
    • C-terminal domain of human pancreatic lipase is required for stability and maximal activity but not colipase reactivation
    • Jennens, M.L. and Lowe, M.E. (1995) C-terminal domain of human pancreatic lipase is required for stability and maximal activity but not colipase reactivation. J. Lipid Res. 36, 1029-1036.
    • (1995) J. Lipid Res. , vol.36 , pp. 1029-1036
    • Jennens, M.L.1    Lowe, M.E.2
  • 29
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and 3-dimensional structure in a large family of esterases, lipases and related proteins
    • Cygler, M. Schrag, J.D., Sussman, J.L., Harel, M., Silman, I., Gentry, M.K. and Doctor, B.P. (1993) Relationship between sequence conservation and 3-dimensional structure in a large family of esterases, lipases and related proteins. Protein Sci. 2, 366-382.
    • (1993) Protein Sci. , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 30
    • 0028034916 scopus 로고
    • Pancreatic triglyceride lipase and colipase - Insights into dietary fat digestion
    • Lowe, M.E. (1994) Pancreatic triglyceride lipase and colipase - insights into dietary fat digestion. Gastroenterology 107, 1524-1536.
    • (1994) Gastroenterology , vol.107 , pp. 1524-1536
    • Lowe, M.E.1
  • 31
    • 0021802672 scopus 로고
    • Limited proteolysis of porcine pancreatic lipase (lability of the Phe 335 - Ala 336 bond towards chymotrypsin)
    • Bousset-Risso, M., Bonicel, J. and Rovery, M. (1985) Limited proteolysis of porcine pancreatic lipase (lability of the Phe 335 - Ala 336 bond towards chymotrypsin). FEBS Lett. 182, 323-326.
    • (1985) FEBS Lett. , vol.182 , pp. 323-326
    • Bousset-Risso, M.1    Bonicel, J.2    Rovery, M.3
  • 32
    • 0030602882 scopus 로고    scopus 로고
    • Mutation of the catalytic site Asp(177) to Glu(177) in human pancreatic lipase produces an active lipase with increased sensitivity to proteases
    • Lowe, M.E. (1996) Mutation of the catalytic site Asp(177) to Glu(177) in human pancreatic lipase produces an active lipase with increased sensitivity to proteases. Biochim. Biophys. Acta 1302, 177-183.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 177-183
    • Lowe, M.E.1
  • 34
    • 0028075638 scopus 로고
    • Elucidating structure-mechanism relationships in lipases - Prospects for predicting and engineering catalytic properties
    • Kazlauskas, R.J. (1994) Elucidating structure-mechanism relationships in lipases - prospects for predicting and engineering catalytic properties. Trends Biotechnol. 12, 464-472.
    • (1994) Trends Biotechnol. , vol.12 , pp. 464-472
    • Kazlauskas, R.J.1
  • 35
    • 0028875755 scopus 로고
    • Human hepatic and lipoprotein lipase - The loop covering the catalytic site mediates lipase substrate specificity
    • Dugi, K.A., Dichek, H.L. and Santamarinafojo, S. (1995) Human hepatic and lipoprotein lipase - the loop covering the catalytic site mediates lipase substrate specificity. J. Biol. Chem. 270, 25 396-25 401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25396-25401
    • Dugi, K.A.1    Dichek, H.L.2    Santamarinafojo, S.3
  • 36
    • 0028152436 scopus 로고
    • A surface loop covering the active site of human pancreatic lipase influences interfacial activation and lipid binding
    • Jennens, M.L. and Lowe, M.E. (1994) A surface loop covering the active site of human pancreatic lipase influences interfacial activation and lipid binding. J. Biol. Chem. 269, 25 470-25 474.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25470-25474
    • Jennens, M.L.1    Lowe, M.E.2
  • 37
    • 0027254059 scopus 로고
    • Picture an enzyme at work
    • Riddihough, G. (1993) Picture an enzyme at work. Nature 362, 793.
    • (1993) Nature , vol.362 , pp. 793
    • Riddihough, G.1
  • 38
    • 0029039839 scopus 로고
    • A twist in the tale of lipolytic enzymes
    • Derewenda, Z.S. (1995) A twist in the tale of lipolytic enzymes. Nature Structural Biol. 2, 347-349.
    • (1995) Nature Structural Biol. , vol.2 , pp. 347-349
    • Derewenda, Z.S.1
  • 40
    • 0021771706 scopus 로고
    • One-step purification of procolipase from human pancreatic juice by immobilized antibodies against human colipase
    • Sternby, B. and Borgstrom, B. (1984) One-step purification of procolipase from human pancreatic juice by immobilized antibodies against human colipase. Biochim. Biophys. Acta 786, 109-112.
    • (1984) Biochim. Biophys. Acta , vol.786 , pp. 109-112
    • Sternby, B.1    Borgstrom, B.2
  • 41
    • 0025763599 scopus 로고
    • The effect of pancreatic procolipase and colipase on pancreatic lipase activation
    • Larsson, A. and Erlanson-Albertsson, C. (1991) The effect of pancreatic procolipase and colipase on pancreatic lipase activation. Biochim. Biophys. Acta 1083, 283-288.
    • (1991) Biochim. Biophys. Acta , vol.1083 , pp. 283-288
    • Larsson, A.1    Erlanson-Albertsson, C.2
  • 43
    • 0024962492 scopus 로고
    • Inhibitory properties and antigenic specificity of monoclonal antibodies to pancreatic lipase
    • de la Fourniere, L., Bosc-Bierne, I., Bellon, B. and Sarda, L. (1989) Inhibitory properties and antigenic specificity of monoclonal antibodies to pancreatic lipase. Biochim. Biophys. Acta 998, 158-166.
    • (1989) Biochim. Biophys. Acta , vol.998 , pp. 158-166
    • De la Fourniere, L.1    Bosc-Bierne, I.2    Bellon, B.3    Sarda, L.4
  • 44
    • 0026687923 scopus 로고
    • Structure of the pancreatic lipase-colipase complex
    • van Tilbeurgh, H., Sarda, L., Verger, R. and Cambillau, C. (1992) Structure of the pancreatic lipase-colipase 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
  • 45
    • 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
  • 46
    • 0028968179 scopus 로고
    • Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase
    • Egloff, M.P., Sarda, L., Verger, R., Cambillau, C. and van Tilbeurgh, H. (1995) Crystallographic study of the structure of colipase and of the interaction with pancreatic lipase. Protein Sci. 4, 44-57.
    • (1995) Protein Sci. , vol.4 , pp. 44-57
    • Egloff, M.P.1    Sarda, L.2    Verger, R.3    Cambillau, C.4    Van Tilbeurgh, H.5
  • 47
    • 0024817012 scopus 로고
    • A cross-linked complex between horse pancreatic lipase and colipase
    • Chaillan, C., Rogalska, E., Chapus, C. and Lombarde, D. (1989) A cross-linked complex between horse pancreatic lipase and colipase. FEES Lett. 257, 443-446.
    • (1989) FEES Lett. , vol.257 , pp. 443-446
    • Chaillan, C.1    Rogalska, E.2    Chapus, C.3    Lombarde, D.4
  • 48
    • 0018801496 scopus 로고
    • Hydrolysis of mixed monomolecular films of triglyceride/lecithin by pancreatic lipase
    • Pieroni, 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
    • Pieroni, G.1    Verger, R.2
  • 49
    • 0018886158 scopus 로고
    • Importance of phospholipids, pancreatic phspholipase a2 and fatty acid for the digestion of dietary fat: In vitro experiments with the porcine enzymes
    • Borgstrom, B. (1980) Importance of phospholipids, pancreatic phspholipase A2 and fatty acid for the digestion of dietary fat: in vitro experiments with the porcine enzymes. Gastroenterology 78, 954-962.
    • (1980) Gastroenterology , vol.78 , pp. 954-962
    • Borgstrom, B.1
  • 51
    • 0023054487 scopus 로고
    • Effect of phosphatidylcholine and free fatty acids on the activity of pancreatic lipase-colipase
    • Larsson, A. and Erlanson-Albertson, C. (1986) Effect of phosphatidylcholine and free fatty acids on the activity of pancreatic lipase-colipase. Biochim. Biophys. Acta 876, 543-550.
    • (1986) Biochim. Biophys. Acta , vol.876 , pp. 543-550
    • Larsson, A.1    Erlanson-Albertson, C.2
  • 52
    • 0004969398 scopus 로고
    • Inhibition of human pancreatic lipase-colipase activity by mixed bile salt-phospholipid micelles
    • Patton, J.S. and Carey, M.C. (1981) Inhibition of human pancreatic lipase-colipase activity by mixed bile salt-phospholipid micelles. Am. J. Physiol. 241, G328-G336.
    • (1981) Am. J. Physiol. , vol.241
    • Patton, J.S.1    Carey, M.C.2
  • 53
    • 0026537542 scopus 로고
    • Physiology and pathophysiology of intestinal absorption
    • Caspary, W.F. (1992) Physiology and pathophysiology of intestinal absorption. Am. J. Clin. Nutr. 55, 299S-308S.
    • (1992) Am. J. Clin. Nutr. , vol.55
    • Caspary, W.F.1
  • 55
    • 73049167589 scopus 로고
    • Physico-chemical state of lipids in intestinal content during their digestion and absorption
    • Hofmann, A.F. and Borgstrom, B. (1962) Physico-chemical state of lipids in intestinal content during their digestion and absorption. Fed. Proc. 21, 43-50.
    • (1962) Fed. Proc. , vol.21 , pp. 43-50
    • Hofmann, A.F.1    Borgstrom, B.2
  • 56
    • 0000422498 scopus 로고
    • The intraluminal phase of fat digestion in man: The lipid content of the micellar and oil phases of intestinal content during fat digestion and absorption
    • Hofmann, A.F. and Borgstrom, B. (1964) The intraluminal phase of fat digestion in man: the lipid content of the micellar and oil phases of intestinal content during fat digestion and absorption. J. Clin. Invest. 43, 247-257.
    • (1964) J. Clin. Invest. , vol.43 , pp. 247-257
    • Hofmann, A.F.1    Borgstrom, B.2
  • 57
    • 0016791571 scopus 로고
    • Isolation and properties of the mixed lipid micelles present in intestinal content during fat digestion in man
    • Mansbach, C.M., Cohen, R.S. and Leff, P.B. (1975) Isolation and properties of the mixed lipid micelles present in intestinal content during fat digestion in man. J. Clin. Invest. 56, 781-791.
    • (1975) J. Clin. Invest. , vol.56 , pp. 781-791
    • Mansbach, C.M.1    Cohen, R.S.2    Leff, P.B.3
  • 58
    • 0018765360 scopus 로고
    • Watching fat digestion
    • Patton, J.S. and Carey, M.S. (1979) Watching fat digestion. Science 204, 145-148.
    • (1979) Science , vol.204 , pp. 145-148
    • Patton, J.S.1    Carey, M.S.2
  • 59
    • 0025239461 scopus 로고
    • Physical-chemical behaviour of dietary and biliary during intestinal digestion and absorption. 1. Phase behaviour and aggregation states of model lipid systems patterned after aqueous duodenal contents of adult human beings
    • Staggers, J.E., Hernell, O., Stafford, R.J. and Carey, M.C. (1990) Physical-chemical behaviour of dietary and biliary during intestinal digestion and absorption. 1. Phase behaviour and aggregation states of model lipid systems patterned after aqueous duodenal contents of adult human beings. Biochemistry 29, 2028-2040.
    • (1990) Biochemistry , vol.29 , pp. 2028-2040
    • Staggers, J.E.1    Hernell, O.2    Stafford, R.J.3    Carey, M.C.4
  • 61
    • 0022605440 scopus 로고
    • A liquid crystalline phase in human intestinal contents during fat digestion
    • Holt, P.R., Fairchild, B.M. and Weiss, J. (1986) A liquid crystalline phase in human intestinal contents during fat digestion. Lipids 21, 444-446.
    • (1986) Lipids , vol.21 , pp. 444-446
    • Holt, P.R.1    Fairchild, B.M.2    Weiss, J.3
  • 62
    • 0022510321 scopus 로고
    • Visualisation by freeze fracture, in vitro and in vivo, of the products of fat digestion
    • Rigler, M.W., Honkanen, R.E. and Patton, J.S. (1986) Visualisation by freeze fracture, in vitro and in vivo, of the products of fat digestion. J. Lipid Res. 27, 836-857.
    • (1986) J. Lipid Res. , vol.27 , pp. 836-857
    • Rigler, M.W.1    Honkanen, R.E.2    Patton, J.S.3
  • 63
    • 0025311288 scopus 로고
    • Epitheal transport of drugs in cell culture. I: A model for studying the passive diffusion of drugs over intestinal absorbtive (Caco-2) cells
    • Artursson, P. (1990) Epitheal transport of drugs in cell culture. I: A model for studying the passive diffusion of drugs over intestinal absorbtive (Caco-2) cells. J. Pharm. Sci. 79, 476-482.
    • (1990) J. Pharm. Sci. , vol.79 , pp. 476-482
    • Artursson, P.1
  • 65
    • 0029161231 scopus 로고
    • The 2.46-angstrom resolution structure of the pancreatic lipase-colipase complex inhibited by a C-11 alkyl phosphonate
    • Egloff, M.P., Marguet, F., Bueno, G., Verger, R., Cambillau, C. and van Tilbeurgh, H. (1995) The 2.46-Angstrom resolution structure of the pancreatic lipase-colipase complex inhibited by a C-11 alkyl phosphonate. Biochemistry 34, 2751-2762.
    • (1995) Biochemistry , vol.34 , pp. 2751-2762
    • Egloff, M.P.1    Marguet, F.2    Bueno, G.3    Verger, R.4    Cambillau, C.5    Van Tilbeurgh, H.6
  • 66
    • 0029898932 scopus 로고    scopus 로고
    • Lipase activation by nonionic detergents - The crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex
    • Hermoso, J., Pignol, D., Kerfelec, B., Crenon, J., Chapus, C. and Fontecillacamps, J.C. (1996) Lipase activation by nonionic detergents - the crystal structure of the porcine lipase-colipase-tetraethylene glycol monooctyl ether complex. J. Biol. Chem. 271, 18007-18016.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18007-18016
    • Hermoso, J.1    Pignol, D.2    Kerfelec, B.3    Crenon, J.4    Chapus, C.5    Fontecillacamps, J.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.