메뉴 건너뛰기




Volumn 7, Issue 3, 1996, Pages 229-236

The secretion of active recombinant human gastric lipase by Saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

LENS CULINARIS; SACCHAROMYCES CEREVISIAE;

EID: 0030151996     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0033     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0024806806 scopus 로고
    • Gastric lipases: Biochemical and physiological studies
    • 1. 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
  • 2
    • 0027250231 scopus 로고
    • Secretion and contribution to lipolysis of gastric and pancreatic lipases during a test meal in humans
    • 2. 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
  • 4
    • 0025356254 scopus 로고
    • The complete digestion of human milk in vitro requires gastric lipase, pancreatic colipase-dependent lipase and bile salt-stimulated lipase
    • 4. Bernbäck, S., Bläckberg, L., and Hernell, O. (1990) The complete digestion of human milk in vitro requires gastric lipase, pancreatic colipase-dependent lipase and bile salt-stimulated lipase. J. Clin. Invest. 85, 1221-1226.
    • (1990) J. Clin. Invest. , vol.85 , pp. 1221-1226
    • Bernbäck, S.1    Bläckberg, L.2    Hernell, O.3
  • 6
    • 0023204739 scopus 로고
    • Role of nonpancreatic lipolytic activity in exocrine pancreatic insufficiency
    • 6. Abrams, C. K., Hamosh, M., Dutta, S. K., Hubbard, V. S., and Hamosh, P. (1987) Role of nonpancreatic lipolytic activity in exocrine pancreatic insufficiency. Gastroenterology 92, 125-129.
    • (1987) Gastroenterology , vol.92 , pp. 125-129
    • Abrams, C.K.1    Hamosh, M.2    Dutta, S.K.3    Hubbard, V.S.4    Hamosh, P.5
  • 7
    • 0026538351 scopus 로고
    • Increased intragastric acid resistant lipase activity and lipolysis in pancreatic steatorrhoea due to cystic fibrosis
    • 7. Balasubramanian, K., Zentler-Munro, P. L., Batten, J. C., and Northfield, T. C. (1992) Increased intragastric acid resistant lipase activity and lipolysis in pancreatic steatorrhoea due to cystic fibrosis. Pancreas 7, 305-310.
    • (1992) Pancreas , vol.7 , pp. 305-310
    • Balasubramanian, K.1    Zentler-Munro, P.L.2    Batten, J.C.3    Northfield, T.C.4
  • 8
    • 0017647730 scopus 로고
    • Fate of orally ingested enzymes in pancreatic insufficiency. Comparison of two dosage schedules
    • 8. DiMagno, E. P., Malagelada, J. R., Go, V. L., and Moertel, C. G. (1977) Fate of orally ingested enzymes in pancreatic insufficiency. Comparison of two dosage schedules. N. Engl. J. Med. 296, 1318-1327.
    • (1977) N. Engl. J. Med. , vol.296 , pp. 1318-1327
    • DiMagno, E.P.1    Malagelada, J.R.2    Go, V.L.3    Moertel, C.G.4
  • 9
    • 0021338655 scopus 로고
    • Effect of intrajejunal acidity on aqueous phase bile acid and lipid concentrations in pancreatic steatorroea due to cystic fibrosis
    • 9. Zentler-Munro, P. L. (1984) Effect of intrajejunal acidity on aqueous phase bile acid and lipid concentrations in pancreatic steatorroea due to cystic fibrosis. Gut 25, 500-507.
    • (1984) Gut , vol.25 , pp. 500-507
    • Zentler-Munro, P.L.1
  • 10
    • 0023492446 scopus 로고
    • Bovine pregastric lipase: A model for the human enzyme with respect to properties relevant to its site of action
    • 10. Bernbäck, S., Hernell, O., and Bläckberg, L. (1987) Bovine pregastric lipase: A model for the human enzyme with respect to properties relevant to its site of action. Biochim. Biophys. Acta 922, 206-207.
    • (1987) Biochim. Biophys. Acta , vol.922 , pp. 206-207
    • Bernbäck, S.1    Hernell, O.2    Bläckberg, L.3
  • 14
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • 14. Hanahan, D. (1983) Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 15
    • 4243728960 scopus 로고
    • Negative regulation of gene expression by mating-type
    • (Walton, E. F., and Yarranton, G. T., Eds.), Blackie, Glasgow, UK
    • 15. Walton, E. F., and Yarranton, G. T. (1989) Negative regulation of gene expression by mating-type, in "The Molecular and Cell Biology of Yeasts" (Walton, E. F., and Yarranton, G. T., Eds.), pp. 43-69, Blackie, Glasgow, UK.
    • (1989) The Molecular and Cell Biology of Yeasts , pp. 43-69
    • Walton, E.F.1    Yarranton, G.T.2
  • 16
    • 0018180547 scopus 로고
    • Transformation of yeast by a replicating hybrid plasmid
    • 16. Beggs, J. D. (1978) Transformation of yeast by a replicating hybrid plasmid. Nature 275, 104-109.
    • (1978) Nature , vol.275 , pp. 104-109
    • Beggs, J.D.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of the structural proteins during the assembly of the head of bacteriophage T4
    • 17. Laemmli, U. (1970) Cleavage of the structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 18
    • 0026775558 scopus 로고
    • Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloprotenases
    • 18. Crabbe, T., Willenbrock, F., Eaton, D., Hynds, P., Carne, A. F., Murphy, G., and Docherty, A. J. P. (1992) Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloprotenases. Biochemistry 31, 8500-8507.
    • (1992) Biochemistry , vol.31 , pp. 8500-8507
    • Crabbe, T.1    Willenbrock, F.2    Eaton, D.3    Hynds, P.4    Carne, A.F.5    Murphy, G.6    Docherty, A.J.P.7
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 19. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 143-147.
    • (1976) Anal. Biochem. , vol.72 , pp. 143-147
    • Bradford, M.M.1
  • 20
    • 0022426981 scopus 로고
    • Determination of absorbtion coefficients of purified proteins by conventional ultraviolet spectrophotometry and chromatography combined with multiwavelength detection
    • 20. Van Iersal, J., Frank Jzn, J., and Duine, J. A. (1985) Determination of absorbtion coefficients of purified proteins by conventional ultraviolet spectrophotometry and chromatography combined with multiwavelength detection. Anal. Biochem. 151, 196-204.
    • (1985) Anal. Biochem. , vol.151 , pp. 196-204
    • Van Iersal, J.1    Frank Jzn, J.2    Duine, J.A.3
  • 21
    • 0023639986 scopus 로고
    • Glycosylation and secretion of human alpha-1-antitrypsin by yeast
    • 21. Moir, D. T., and Dumais, D. R. (1987) Glycosylation and secretion of human alpha-1-antitrypsin by yeast. Gene 56, 209-217.
    • (1987) Gene , vol.56 , pp. 209-217
    • Moir, D.T.1    Dumais, D.R.2
  • 22
    • 0027301394 scopus 로고
    • Purification of human gastric lipase by immunoaffinity and quantification of this enzyme in duodenal contents using a new ELISA procedure
    • 22. Aoubala, M., Douchet, I., Laugier, R., Hirn, M., Verger, R., and DeCaro, A. (1993) Purification of human gastric lipase by immunoaffinity and quantification of this enzyme in duodenal contents using a new ELISA procedure. Biochim. Biophys. Acta 1169, 183-188.
    • (1993) Biochim. Biophys. Acta , vol.1169 , pp. 183-188
    • Aoubala, M.1    Douchet, I.2    Laugier, R.3    Hirn, M.4    Verger, R.5    DeCaro, A.6
  • 23
    • 0021764073 scopus 로고
    • Secretion of phospholipase B from Saccharomyces cerevisiae
    • 23. Witt, W., Mertsching, A., and König, E. (1984) Secretion of phospholipase B from Saccharomyces cerevisiae. Biochim. Biophys. Acta 795, 117-124.
    • (1984) Biochim. Biophys. Acta , vol.795 , pp. 117-124
    • Witt, W.1    Mertsching, A.2    König, E.3
  • 24
    • 0022481842 scopus 로고
    • Expression of synthetic human-lysozyme gene in Saccharomyces cerevisiae: Use of a synthetic chicken-lysozyme signal sequence for secretion and processing
    • 24. Jigami, Y., Muraki, M., Harada, N., and Tanaka, H. (1986) Expression of synthetic human-lysozyme gene in Saccharomyces cerevisiae: Use of a synthetic chicken-lysozyme signal sequence for secretion and processing. Gene 43, 273-279.
    • (1986) Gene , vol.43 , pp. 273-279
    • Jigami, Y.1    Muraki, M.2    Harada, N.3    Tanaka, H.4
  • 26
    • 0024548511 scopus 로고
    • Secretion of active full-and half-length human secretory leukocyte protease inhibitor by Saccharomyces cerevisiae
    • 26. Stetler, G. L., Forsyth, C., Gleason, T., Wilson, J., and Thompson, R. C. (1989) Secretion of active full-and half-length human secretory leukocyte protease inhibitor by Saccharomyces cerevisiae. Bio/Technology 7, 55-60.
    • (1989) Bio/Technology , vol.7 , pp. 55-60
    • Stetler, G.L.1    Forsyth, C.2    Gleason, T.3    Wilson, J.4    Thompson, R.C.5
  • 27
    • 0025809077 scopus 로고
    • Passage of molecules through yeast cell walls: A brief essay-review
    • 27. De Nobel, J. G., and Barnett, J. A. (1991) Passage of molecules through yeast cell walls: a brief essay-review. Yeast 7, 313-323.
    • (1991) Yeast , vol.7 , pp. 313-323
    • De Nobel, J.G.1    Barnett, J.A.2
  • 28
    • 0001930052 scopus 로고
    • Extracellular microbial lipases
    • (Fogarty, W. M., Ed.), Applied Science Publishers, London, UK
    • 28. Macrae, A. R. (1983) Extracellular microbial lipases, in "Microbial Enzymes and Biotechnology" (Fogarty, W. M., Ed.), pp. 225-250, Applied Science Publishers, London, UK.
    • (1983) Microbial Enzymes and Biotechnology , pp. 225-250
    • Macrae, A.R.1
  • 29
    • 0000233599 scopus 로고
    • Purification and some properties of cell-bound lipase from Saccharomycopsis lipolytica
    • 29. Ota, Y., Gomi, K., Kato, S., Sugiura, T., and Minoda, Y. (1982) Purification and some properties of cell-bound lipase from Saccharomycopsis lipolytica. Agric. Biol. Chem. 46, 2885-2893.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 2885-2893
    • Ota, Y.1    Gomi, K.2    Kato, S.3    Sugiura, T.4    Minoda, Y.5
  • 31
    • 0024727394 scopus 로고
    • Rhizomucor miehei triglyceride lipase is processed and secreted from transformed Aspergillus oryzae
    • 31. Huge-Jensen, B., Anderson, F., Christensen, T., Christensen, M., Thim, L., and Boel, E. (1989) Rhizomucor miehei triglyceride lipase is processed and secreted from transformed Aspergillus oryzae. Lipids 24, 781-785.
    • (1989) Lipids , vol.24 , pp. 781-785
    • Huge-Jensen, B.1    Anderson, F.2    Christensen, T.3    Christensen, M.4    Thim, L.5    Boel, E.6
  • 35
    • 15444377148 scopus 로고
    • Yeast systems for the commercial production of proteins
    • 35. Buckholz, R. G., and Gleeson, M. A. G. (1991) Yeast systems for the commercial production of proteins. Bio/Technology 9, 1067-1072.
    • (1991) Bio/Technology , vol.9 , pp. 1067-1072
    • Buckholz, R.G.1    Gleeson, M.A.G.2
  • 36
    • 0027227838 scopus 로고
    • Expression systems: A user's guide
    • 36. Hodgson, J. (1993) Expression systems: A user's guide. Bio/Technology 11, 887-893.
    • (1993) Bio/Technology , vol.11 , pp. 887-893
    • Hodgson, J.1
  • 37
    • 0021934311 scopus 로고
    • Single-step purification and amino acid and lipid composition of purified acid lipase from human gastric juice
    • 37. Tirrupathi, C., and Balasubramanian, K. A. (1985) Single-step purification and amino acid and lipid composition of purified acid lipase from human gastric juice. Indian J. Biochem. Biophys. 22, 111-114.
    • (1985) Indian J. Biochem. Biophys. , vol.22 , pp. 111-114
    • Tirrupathi, C.1    Balasubramanian, K.A.2
  • 39
    • 0002180797 scopus 로고
    • Yeast cell wall and cell surface
    • (Strathern, J. N., Jones, E. W., and Broach, J. R., Eds.), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • 39. Ballou, C. E. (1982) Yeast cell wall and cell surface, in "The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression" (Strathern, J. N., Jones, E. W., and Broach, J. R., Eds.), pp. 335-360, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (1982) The Molecular Biology of the Yeast Saccharomyces: Metabolism and Gene Expression , pp. 335-360
    • Ballou, C.E.1
  • 40
    • 0023875673 scopus 로고
    • Efficient secretion of two cellobiohydrolases by Saccharomyces cerevisiae
    • 40. Penttilä, M. E., André, L., Lehtovaara, P., Bailey, M., Teeri, T. T., and Knowles, J. K. C. (1988) Efficient secretion of two cellobiohydrolases by Saccharomyces cerevisiae. Gene 63, 103-112.
    • (1988) Gene , vol.63 , pp. 103-112
    • Penttilä, M.E.1    André, L.2    Lehtovaara, P.3    Bailey, M.4    Teeri, T.T.5    Knowles, J.K.C.6
  • 41
    • 0011846938 scopus 로고
    • Secretion of human tissue-type plasminogen activator (tPA) by strains of Saccharomyces cerevisiae: Initial characterization of the secreted material
    • Spec. Iss. S1-S520
    • 41. Gill, G. S., Zaworski, P. G., Marotti, K. R., and Rehberg, E. F. (1988) Secretion of human tissue-type plasminogen activator (tPA) by strains of Saccharomyces cerevisiae: Initial characterization of the secreted material. Yeast 4 (Spec. Iss. S1-S520), S148.
    • (1988) Yeast , vol.4
    • Gill, G.S.1    Zaworski, P.G.2    Marotti, K.R.3    Rehberg, E.F.4
  • 42
    • 0020522151 scopus 로고
    • Glycoprotein biosynthesis in yeast. Protein conformation affects processing of high mannose oligosaccharides on carboxypeptidase Y and invertase
    • 42. Trimble, R. B., Maley, F., and Chu, F. K. (1983) Glycoprotein biosynthesis in yeast. Protein conformation affects processing of high mannose oligosaccharides on carboxypeptidase Y and invertase. J. Biol. Chem. 258, 2562-2567.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2562-2567
    • Trimble, R.B.1    Maley, F.2    Chu, F.K.3
  • 43
    • 0022898326 scopus 로고
    • Protein sorting in yeast: Mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway
    • 43. Rothman, J. H., and Stevens, T. H. (1986) Protein sorting in yeast: mutants defective in vacuole biogenesis mislocalize vacuolar proteins into the late secretory pathway. Cell 47, 1041-1051.
    • (1986) Cell , vol.47 , pp. 1041-1051
    • Rothman, J.H.1    Stevens, T.H.2
  • 44
    • 0024345811 scopus 로고
    • Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity
    • 44. Bernbäck, S., and Bläckberg, L. (1989) Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity. Eur. J. Biochem. 180, 495-499.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 495-499
    • Bernbäck, S.1    Bläckberg, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.