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Volumn 267, Issue 9, 2000, Pages 2573-2580

Purification and characterization of active recombinant human napsin A

Author keywords

Aspartic proteinases; Fluorescence resonance energy transfer; Kinetics; PH optimum; Propeptide

Indexed keywords

ASPARTIC PROTEINASE; RECOMBINANT ENZYME;

EID: 0034084897     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01268.x     Document Type: Article
Times cited : (16)

References (38)
  • 1
    • 0032410105 scopus 로고    scopus 로고
    • Napsins. New human aspartic proteinases: Distinction between two closely related genes
    • 1. Tatnell, P.J., Powell, D.J., Hill, J., Smith, T.S., Tew, D.G. & Kay, J. (1998) Napsins. New human aspartic proteinases: distinction between two closely related genes. FEBS Lett. 441, 43-48.
    • (1998) FEBS Lett. , vol.441 , pp. 43-48
    • Tatnell, P.J.1    Powell, D.J.2    Hill, J.3    Smith, T.S.4    Tew, D.G.5    Kay, J.6
  • 2
    • 0032740358 scopus 로고    scopus 로고
    • Human napsin a: Expression, immunochemical detection, and tissue localization
    • 2. Schauer-Vukasinovic, V., Bur, D., Kling, D., Grüninger, F. & Giller, T. (1999) Human napsin A: expression, immunochemical detection, and tissue localization. FEBS Lett. 462, 135-139.
    • (1999) FEBS Lett. , vol.462 , pp. 135-139
    • Schauer-Vukasinovic, V.1    Bur, D.2    Kling, D.3    Grüninger, F.4    Giller, T.5
  • 3
    • 0027978637 scopus 로고
    • Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus
    • 3. Nilsson, T. & Warren, G. (1994) Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell Biol. 6, 517-521.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 517-521
    • Nilsson, T.1    Warren, G.2
  • 5
    • 0029120229 scopus 로고
    • Cathepsin E and D: Biosynthesis, processing and subcellular localization
    • 5. Yamamoto, K. (1995) Cathepsin E and D: biosynthesis, processing and subcellular localization. Adv. Exp. Med. Biol. 362, 223-229.
    • (1995) Adv. Exp. Med. Biol. , vol.362 , pp. 223-229
    • Yamamoto, K.1
  • 6
    • 0018769429 scopus 로고
    • Characterization of human pepsin I obtained from purified gastric pepsinogen I
    • 6. Becker, T. & Rapp, W. (1979) Characterization of human pepsin I obtained from purified gastric pepsinogen I. Klin. Wochenschr. 57, 711-718.
    • (1979) Klin. Wochenschr. , vol.57 , pp. 711-718
    • Becker, T.1    Rapp, W.2
  • 7
    • 0026482923 scopus 로고
    • Kinetic studies on recombinant human renin with recombinant human angiotensinogen derived from Chinese hamster ovary cells
    • 7. Hatae, T., Takimoto, E., Fukamizu, A. & Murakami, K. (1992) Kinetic studies on recombinant human renin with recombinant human angiotensinogen derived from Chinese hamster ovary cells. Biomed. Res. 13, 381-383.
    • (1992) Biomed. Res. , vol.13 , pp. 381-383
    • Hatae, T.1    Takimoto, E.2    Fukamizu, A.3    Murakami, K.4
  • 8
    • 0026651507 scopus 로고
    • Biological and clinical significance of cathepsin D in breast cancer
    • 8. Rochefort, H. (1992) Biological and clinical significance of cathepsin D in breast cancer. Acta Oncologica 31, 125-130.
    • (1992) Acta Oncologica , vol.31 , pp. 125-130
    • Rochefort, H.1
  • 12
    • 0030798898 scopus 로고    scopus 로고
    • Pepsinogens and pepsins from house musk shrew, Suncis murinus: Purification, characterization, determination of the amino-acid sequences of the activation segments, and analysis of proteolytic specificities
    • 12. Narita, Y., Oda, S., Moriyama, A., Takenaka, O. & Kageyama, T. (1997) Pepsinogens and pepsins from house musk shrew, Suncis murinus: purification, characterization, determination of the amino-acid sequences of the activation segments, and analysis of proteolytic specificities. J. Biochem. (Tokyo) 121, 1010-1017.
    • (1997) J. Biochem. (Tokyo) , vol.121 , pp. 1010-1017
    • Narita, Y.1    Oda, S.2    Moriyama, A.3    Takenaka, O.4    Kageyama, T.5
  • 13
    • 53249132917 scopus 로고    scopus 로고
    • Purification and characterization of cathepsin D from normal human breast tissue
    • 13. Wright, L.M., Levy, E.S., Patel, N.P. & Alhadeff, J.A. (1997) Purification and characterization of cathepsin D from normal human breast tissue. J. Protein Chem. 16, 171-181.
    • (1997) J. Protein Chem. , vol.16 , pp. 171-181
    • Wright, L.M.1    Levy, E.S.2    Patel, N.P.3    Alhadeff, J.A.4
  • 14
    • 0024451999 scopus 로고
    • Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme
    • 14. Conner, G.E. (1989) Isolation of procathepsin D from mature cathepsin D by pepstatin affinity chromatography. Autocatalytic proteolysis of the zymogen form of the enzyme. Biochem. J. 263, 601-604.
    • (1989) Biochem. J. , vol.263 , pp. 601-604
    • Conner, G.E.1
  • 16
    • 0021233715 scopus 로고
    • Purification of pepsins and cathepsin D by affinity chromatography on Sepharose 4B with an immobilized synthetic inhibitor
    • 16. Pohl, J., Zaoral, M., Jindra, A. Jr & Kostka, V. (1984) Purification of pepsins and cathepsin D by affinity chromatography on Sepharose 4B with an immobilized synthetic inhibitor. Anal. Biochem. 139, 265-271.
    • (1984) Anal. Biochem. , vol.139 , pp. 265-271
    • Pohl, J.1    Zaoral, M.2    Jindra A., Jr.3    Kostka, V.4
  • 18
    • 0032521597 scopus 로고    scopus 로고
    • One-step purification of cahtepsin D by affinity chromatography using immobilized propeptide sequences
    • 18. Wittlin, S., Rosel, J. & Stover, D.R. (1998) One-step purification of cahtepsin D by affinity chromatography using immobilized propeptide sequences. Eur. J. Biochem. 252, 530-536.
    • (1998) Eur. J. Biochem. , vol.252 , pp. 530-536
    • Wittlin, S.1    Rosel, J.2    Stover, D.R.3
  • 19
    • 0025874201 scopus 로고
    • Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen
    • 19. Fusek, M., Mares, M., Vagner, J., Voburka, Z. & Baudys, M. (1991) Inhibition of aspartic proteinases by propart peptides of human procathepsin D and chicken pepsinogen. FEBS Lett. 287, 160-162.
    • (1991) FEBS Lett. , vol.287 , pp. 160-162
    • Fusek, M.1    Mares, M.2    Vagner, J.3    Voburka, Z.4    Baudys, M.5
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 22. Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 12044258245 scopus 로고
    • 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive
    • 23. Carpino, L.A. (1993) 1-Hydroxy-7-azabenzotriazole. An efficient peptide coupling additive. J. Amer. Chem. Soc. 115, 4397-4398.
    • (1993) J. Amer. Chem. Soc. , vol.115 , pp. 4397-4398
    • Carpino, L.A.1
  • 24
    • 0030811433 scopus 로고    scopus 로고
    • Structural characterization of activation 'intermediate 2' on the pathway to human gastriesin
    • 24. Khan, A.R., Cherney, M.M., Tarasova, N.I. & James, M.N.G. (1997) Structural characterization of activation 'intermediate 2' on the pathway to human gastriesin. Nat. Struct. Biol. 4, 1010-1015.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1010-1015
    • Khan, A.R.1    Cherney, M.M.2    Tarasova, N.I.3    James, M.N.G.4
  • 25
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • 25. Khan, A.R. & James, M.N. (1998) Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 7, 815-836.
    • (1998) Protein Sci. , vol.7 , pp. 815-836
    • Khan, A.R.1    James, M.N.2
  • 26
    • 0023209825 scopus 로고
    • Evolution in the structure and function of aspartic proteases
    • 26. Tang, J. & Wong, R.N.S. (1987) Evolution in the structure and function of aspartic proteases. J. Cell. Biochem. 33, 53-63.
    • (1987) J. Cell. Biochem. , vol.33 , pp. 53-63
    • Tang, J.1    Wong, R.N.S.2
  • 28
    • 0027530694 scopus 로고
    • Procathepsin D cannot autoactivate to cathepsin D at acidic pH
    • 28. Larsen, L.B., Boisen, A. & Petersen, T.E. (1993) Procathepsin D cannot autoactivate to cathepsin D at acidic pH. FEBS Lett. 319, 54-58.
    • (1993) FEBS Lett. , vol.319 , pp. 54-58
    • Larsen, L.B.1    Boisen, A.2    Petersen, T.E.3
  • 29
    • 0027414640 scopus 로고
    • Two crystal structures for cathepsin D: The lysosomal targeting signal and active site
    • 29. Metcalf, P. & Fusek, M. (1993) Two crystal structures for cathepsin D: the lysosomal targeting signal and active site. EMBO J. 12, 1293-1302.
    • (1993) EMBO J. , vol.12 , pp. 1293-1302
    • Metcalf, P.1    Fusek, M.2
  • 30
    • 0030915764 scopus 로고    scopus 로고
    • Cloning, expression and characterization of murine procathepsin E
    • 30. Tatnell, P.J., Lees, W.E. & Kay, J. (1997) Cloning, expression and characterization of murine procathepsin E. FEBS Lett. 408, 62-66.
    • (1997) FEBS Lett. , vol.408 , pp. 62-66
    • Tatnell, P.J.1    Lees, W.E.2    Kay, J.3
  • 31
    • 0022766162 scopus 로고
    • A systematic series of synthetic chromophoric substrates for aspartic proteinases
    • 31. Dunn, B.M., Jimenez, M., Parten, B.F., Valler, M.J., Rolph, C.E. & Kay, J. (1986) A systematic series of synthetic chromophoric substrates for aspartic proteinases. Biochem. J. 237, 899-906.
    • (1986) Biochem. J. , vol.237 , pp. 899-906
    • Dunn, B.M.1    Jimenez, M.2    Parten, B.F.3    Valler, M.J.4    Rolph, C.E.5    Kay, J.6
  • 32
    • 0032170893 scopus 로고    scopus 로고
    • Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library
    • 32. Peterson, J.J. & Meares, C.F. (1998) Cathepsin substrates as cleavable peptide linkers in bioconjugates, selected from a fluorescence quench combinatorial library. Bioconj. Chem. 9, 618-626.
    • (1998) Bioconj. Chem. , vol.9 , pp. 618-626
    • Peterson, J.J.1    Meares, C.F.2
  • 33
    • 0023784153 scopus 로고
    • Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E
    • 33. Jupp, R.A., Richards, A.D., Kay, J., Dunn, B.M., Wyckoff, J.B., Samloff, I.M. & Yamamoto, K. (1988) Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E. Biochem. J. 254, 895-898.
    • (1988) Biochem. J. , vol.254 , pp. 895-898
    • Jupp, R.A.1    Richards, A.D.2    Kay, J.3    Dunn, B.M.4    Wyckoff, J.B.5    Samloff, I.M.6    Yamamoto, K.7
  • 34
    • 0025342579 scopus 로고
    • Substrate specificity of recombinant human renal renin: Effect of histidine in the P2 subsite on pH dependence
    • 34. Green, D.W., Aykent, S., Gierse, J.K. & Zupek, M.E. (1990) Substrate specificity of recombinant human renal renin: effect of histidine in the P2 subsite on pH dependence. Biochemistry 29, 3126-3133.
    • (1990) Biochemistry , vol.29 , pp. 3126-3133
    • Green, D.W.1    Aykent, S.2    Gierse, J.K.3    Zupek, M.E.4
  • 35
    • 0015326896 scopus 로고
    • The inhibition of tissue acid proteinases by pepstatin
    • 35. Barrett, A.J. & Dingle, J.T. (1972) The inhibition of tissue acid proteinases by pepstatin. Biochem. J. 127, 439-441.
    • (1972) Biochem. J. , vol.127 , pp. 439-441
    • Barrett, A.J.1    Dingle, J.T.2
  • 36
    • 0015972948 scopus 로고
    • A simple graphical method for determining the inhibition constants of mixed, uncompetitive and noncompetitive inhibitors
    • 36. Cornish-Bowden, A. (1974) A simple graphical method for determining the inhibition constants of mixed, uncompetitive and noncompetitive inhibitors. Biochem. J. 137, 143-144.
    • (1974) Biochem. J. , vol.137 , pp. 143-144
    • Cornish-Bowden, A.1


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