메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages 343-348

Monitoring stepwise proteolytic degradation of peptides by supramolecular domino tandem assays and mass spectrometry for trypsin and leucine aminopeptidase

Author keywords

Cucurbituril; Enzyme assays; Enzymes; Fluorescence; Macrocycles; Mass spectrometry; Proteases; Supramolecular chemistry

Indexed keywords

ACRIDINE ORANGE; CUCURBITURIL; CYTOSOL AMINOPEPTIDASE; PHENYLALANINE; RECEPTOR; TRYPSIN; UNCLASSIFIED DRUG;

EID: 84859235950     PISSN: 1934578X     EISSN: 15559475     Source Type: Journal    
DOI: 10.1177/1934578x1200700315     Document Type: Article
Times cited : (20)

References (59)
  • 1
    • 0037803570 scopus 로고    scopus 로고
    • Human and mouse proteases: A comparative genomic approach
    • DOI 10.1038/nrg1111
    • Puente XS, Sanchez LM, Overall CM, Lopez-Otin C. (2003) Human and mouse proteases: A comparative genomic approach. Nature Reviews Genetics, 4, 544-558. (Pubitemid 36781345)
    • (2003) Nature Reviews Genetics , vol.4 , Issue.7 , pp. 544-558
    • Puente, X.S.1    Sanchez, L.M.2    Overall, C.M.3    Lopez-Otin, C.4
  • 2
    • 44649129938 scopus 로고    scopus 로고
    • Novel assays for proteases using green fluorescent protein-tagged substrate immobilized on a membrane disk
    • (a) Aoki T, Tsuchida S, Yahara T, Hamaue N. (2008) Novel assays for proteases using green fluorescent protein-tagged substrate immobilized on a membrane disk. Analytical Biochemistry, 378, 132-137;
    • (2008) Analytical Biochemistry , vol.378 , pp. 132-137
    • Aoki, T.1    Tsuchida, S.2    Yahara, T.3    Hamaue, N.4
  • 4
    • 0029147294 scopus 로고
    • Automation of a high-performance liquid chromatography-based enzyme assay: Evaluation of inhibition constants for human immunodeficiency virus-1 protease inhibitors
    • (c) Pazhanisamy S, Stuver CM, Livingston DJ. (1995) Automation of a high-performance liquid chromatography-based enzyme assay: evaluation of inhibition constants for human immunodeficiency virus-1 protease inhibitors. Analytcial Biochemistry, 229, 48-53;
    • (1995) Analytcial Biochemistry , vol.229 , pp. 48-53
    • Pazhanisamy, S.1    Stuver, C.M.2    Livingston, D.J.3
  • 5
    • 68449090012 scopus 로고    scopus 로고
    • Monitoring peptidase activities in complex proteomes by MALDI-TOF mass spectrometry
    • (d) Villanueva J, Nazarian A, Lawlor K, Tempst P. (2009) Monitoring peptidase activities in complex proteomes by MALDI-TOF mass spectrometry. Nature Protocols, 4, 1167-1183;
    • (2009) Nature Protocols , vol.4 , pp. 1167-1183
    • Villanueva, J.1    Nazarian, A.2    Lawlor, K.3    Tempst, P.4
  • 6
    • 2342478508 scopus 로고    scopus 로고
    • Application of in-gel protease assay in biological sample: Characterization and identification of urokinase-type plasminogen activator (uPA) in secreted proteins from a prostate cancer cell line PC-3
    • (e) Zhao Z, Raftery MJ, Niu XM, Daja MM, Russell PJ. (2004) Application of in-gel protease assay in a biological sample: characterization and identification of urokinase-type plasminogen activator (uPA) in secreted proteins from a prostate cancer cell line PC-3. Electrophoresis, 25, 1142-1148. (Pubitemid 38578956)
    • (2004) Electrophoresis , vol.25 , Issue.7-8 , pp. 1142-1148
    • Zhao, Z.1    Raftery, M.J.2    Niu, X.M.3    Daja, M.M.4    Russell, P.J.5
  • 7
    • 0021965335 scopus 로고
    • An overview of protease specificity and catalytic mechanisms: Aspects related to nomenclature and classification
    • McDonald JK. (1985) An overview of protease specificity and catalytic mechanisms: aspects related to nomenclature and classification. The Histochemical Journal, 17, 773-785.
    • (1985) The Histochemical Journal , vol.17 , pp. 773-785
    • McDonald, J.K.1
  • 9
    • 33845624672 scopus 로고    scopus 로고
    • Design of peptide substrates for nanosecond time-resolved fluorescence assays of proteases: 2,3-diazabicyclo[2.2.2]oct-2-ene as a noninvasive fluorophore
    • (b) Hennig A, Florea M, Roth D, Enderle T, Nau WM. (2007) Design of peptide substrates for nanosecond time-resolved fluorescence assays of proteases: 2,3-diazabicyclo[2.2.2]oct-2-ene as a noninvasive fluorophore. Analytcial Biochemistry, 360, 255-265;
    • (2007) Analytcial Biochemistry , vol.360 , pp. 255-265
    • Hennig, A.1    Florea, M.2    Roth, D.3    Enderle, T.4    Nau, W.M.5
  • 10
    • 67349163726 scopus 로고    scopus 로고
    • Novel and highly sensitive fluorescent assay for leucine aminopeptidases
    • (c) Huang H, Tanaka H, Hammock BD, Morisseau C. (2009) Novel and highly sensitive fluorescent assay for leucine aminopeptidases. Analytical Biochemistry, 391, 11-16;
    • (2009) Analytical Biochemistry , vol.391 , pp. 11-16
    • Huang, H.1    Tanaka, H.2    Hammock, B.D.3    Morisseau, C.4
  • 11
    • 4444254474 scopus 로고    scopus 로고
    • Highly sensitive protease assay using fluorescence quenching of peptide probes based on photoinduced electron transfer
    • (d) Marmé N, Knemeyer JP, Wolfrum J, Sauer M. (2004) Highly sensitive protease assay using fluorescence quenching of peptide probes based on photoinduced electron transfer. Angewandte Chemie International Edition, 43, 3798-3801;
    • (2004) Angewandte Chemie International Edition , vol.43 , pp. 3798-3801
    • Marmé, N.1    Knemeyer, J.P.2    Wolfrum, J.3    Sauer, M.4
  • 12
    • 33646807480 scopus 로고    scopus 로고
    • Nanosecond time-resolved fluorescence protease assays
    • (e) Hennig A, Roth D, Enderle T, Nau WM. (2006) Nanosecond time-resolved fluorescence protease assays. Chembiochem, 7, 733-737;
    • (2006) Chembiochem , vol.7 , pp. 733-737
    • Hennig, A.1    Roth, D.2    Enderle, T.3    Nau, W.M.4
  • 13
    • 0037687921 scopus 로고    scopus 로고
    • A green fluorescent chemosensor for amino acids provides a versatile high-throughput screening (HTS) assay for proteases
    • DOI 10.1016/S0960-894X(03)00280-4
    • (f) Dean KE, Klein G, Renaudet O, Reymond JL. (2003) A green fluorescent chemosensor for amino acids provides a versatile high-throughput screening (HTS) assay for proteases. Bioorganic & Medicinal Chemistry Letters, 13, 1653-1656. (Pubitemid 36561134)
    • (2003) Bioorganic and Medicinal Chemistry Letters , vol.13 , Issue.10 , pp. 1653-1656
    • Dean, K.E.S.1    Klein, G.2    Renaudet, O.3    Reymond, J.-L.4
  • 14
    • 23244467785 scopus 로고    scopus 로고
    • Monitoring enzymatic conversions by mass spectrometry: A critical review
    • DOI 10.1007/s00216-005-3305-2
    • Liesener A, Karst U. (2005) Monitoring enzymatic conversions by mass spectrometry: a critical review. Analytical and Bioanalytcial Chemistry, 382, 1451-1464. (Pubitemid 41090448)
    • (2005) Analytical and Bioanalytical Chemistry , vol.382 , Issue.7 , pp. 1451-1464
    • Liesener, A.1    Karst, U.2
  • 15
    • 34547629235 scopus 로고    scopus 로고
    • Label-free continuous enzyme assays with macrocycle-fluorescent dye complexes
    • (a) Hennig A, Bakirci H, Nau WM. (2007) Label-free continuous enzyme assays with macrocycle-fluorescent dye complexes. Nature Methods, 4, 629-632;
    • (2007) Nature Methods , vol.4 , pp. 629-632
    • Hennig, A.1    Bakirci, H.2    Nau, W.M.3
  • 16
    • 68849087539 scopus 로고    scopus 로고
    • Substrate-selective supramolecular tandem assays: Monitoring enzyme inhibition of arginase and diamine oxidase by fluorescent dye displacement from calixarene and cucurbituril macrocycles
    • (b) Nau WM, Ghale G, Hennig A, Bakirci H, Bailey DM. (2009) Substrate-selective supramolecular tandem assays: monitoring enzyme inhibition of arginase and diamine oxidase by fluorescent dye displacement from calixarene and cucurbituril macrocycles. Journal of the American Chemical Society, 131, 11558-11570;
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 11558-11570
    • Nau, W.M.1    Ghale, G.2    Hennig, A.3    Bakirci, H.4    Bailey, D.M.5
  • 17
    • 77149152800 scopus 로고    scopus 로고
    • Implementation of anion-receptor macrocycles in supramolecular tandem assays for enzymes involving nucleotides as substrates, products, and cofactors
    • (c) Florea M, Nau WM. (2010) Implementation of anion-receptor macrocycles in supramolecular tandem assays for enzymes involving nucleotides as substrates, products, and cofactors. Organic & Biomolecular Chemistry, 8, 1033-1039;
    • (2010) Organic & Biomolecular Chemistry , vol.8 , pp. 1033-1039
    • Florea, M.1    Nau, W.M.2
  • 18
    • 79955881748 scopus 로고    scopus 로고
    • Determining protease substrate selectivity and inhibition by label-free supramolecular tandem enzyme assays
    • (d) Ghale G, Ramalingam V, Urbach AR, Nau WM. (2011) Determining protease substrate selectivity and inhibition by label-free supramolecular tandem enzyme assays. Journal of the American Chemical Society, 133, 7528-7535;
    • (2011) Journal of the American Chemical Society , vol.133 , pp. 7528-7535
    • Ghale, G.1    Ramalingam, V.2    Urbach, A.R.3    Nau, W.M.4
  • 19
    • 80053482348 scopus 로고    scopus 로고
    • Operational calixarene-based fluorescent sensing systems for choline and acetylcholine and their application to enzymatic reactions
    • (e) Guo DS, Uzunova VD, Su X, Liu Y, Nau WM. (2011) Operational calixarene-based fluorescent sensing systems for choline and acetylcholine and their application to enzymatic reactions. Chemical Science, 2, 1722-1734.
    • (2011) Chemical Science , vol.2 , pp. 1722-1734
    • Guo, D.S.1    Uzunova, V.D.2    Su, X.3    Liu, Y.4    Nau, W.M.5
  • 20
    • 4043177181 scopus 로고    scopus 로고
    • Using indicator-displacement assays in test strips and to follow reaction kinetics
    • (a) Nguyen BT, Wiskur SL, Anslyn EV. (2004) Using indicator-displacement assays in test strips and to follow reaction kinetics. Organic Letters, 6, 2499-2501;
    • (2004) Organic Letters , vol.6 , pp. 2499-2501
    • Nguyen, B.T.1    Wiskur, S.L.2    Anslyn, E.V.3
  • 21
    • 34248360790 scopus 로고    scopus 로고
    • Using an indicator displacement assay to monitor glucose oxidase activity in blood serum
    • (b) Zhang T, Anslyn EV. (2007) Using an indicator displacement assay to monitor glucose oxidase activity in blood serum. Organic Letters, 9, 1627-1629;
    • (2007) Organic Letters , vol.9 , pp. 1627-1629
    • Zhang, T.1    Anslyn, E.V.2
  • 22
    • 83755178222 scopus 로고    scopus 로고
    • Fluorescent dyes and their supramolecular host-guest complexes with macrocycles in aqueous solution
    • (c) Dsouza RN, Pischel U, Nau WM. (2011) Fluorescent dyes and their supramolecular host-guest complexes with macrocycles in aqueous solution, Chemical Reviews, 111, 7941-7980.
    • (2011) Chemical Reviews , vol.111 , pp. 7941-7980
    • Dsouza, R.N.1    Pischel, U.2    Nau, W.M.3
  • 23
    • 41749099029 scopus 로고    scopus 로고
    • Complexation of acridine orange by cucurbit[7]uril and beta-cyclodextrin: Photophysical effects and pKa shifts
    • (a) Shaikh M, Mohanty J, Singh PK, Nau WM, Pal H. (2008) Complexation of acridine orange by cucurbit[7]uril and beta-cyclodextrin: photophysical effects and pKa shifts. Photochemical and Photobiological Sciences, 7, 408-414;
    • (2008) Photochemical and Photobiological Sciences , vol.7 , pp. 408-414
    • Shaikh, M.1    Mohanty, J.2    Singh, P.K.3    Nau, W.M.4    Pal, H.5
  • 27
    • 0035977209 scopus 로고    scopus 로고
    • Controlling factors in the synthesis of cucurbituril and its homologues
    • (c) Day A, Arnold AP, Blanch RJ, Snushall B. (2001) Controlling factors in the synthesis of cucurbituril and its homologues. Journal of Organic Chemistry, 66, 8094-8100;
    • (2001) Journal of Organic Chemistry , vol.66 , pp. 8094-8100
    • Day, A.1    Arnold, A.P.2    Blanch, R.J.3    Snushall, B.4
  • 28
    • 2342447320 scopus 로고    scopus 로고
    • Cucurbiturils: Molecular nanocapsules for time-resolved fluorescence-based assays
    • (d) Márquez C, Huang F, Nau WM. (2004) Cucurbiturils: Molecular nanocapsules for time-resolved fluorescence-based assays. Ieee Transactions on Nanobioscience, 3, 39-45.
    • (2004) Ieee Transactions on Nanobioscience , vol.3 , pp. 39-45
    • Márquez, C.1    Huang, F.2    Nau, W.M.3
  • 31
    • 79957562110 scopus 로고    scopus 로고
    • Deep inside cucurbiturils: Physical properties and volumes of their inner cavity determine the hydrophobic driving force for host-guest complexation
    • (c) Nau WM, Florea M, Assaf KI. (2011) Deep inside cucurbiturils: Physical properties and volumes of their inner cavity determine the hydrophobic driving force for host-guest complexation. Israel Journal of Chemistry, 51, 559-577.
    • (2011) Israel Journal of Chemistry , vol.51 , pp. 559-577
    • Nau, W.M.1    Florea, M.2    Assaf, K.I.3
  • 33
    • 0032483698 scopus 로고    scopus 로고
    • Sequence-selective evaluation of peptide side-chain interaction. New artificial receptors for selective recognition in water
    • (a) Hossain MA, Schneider HJ. (1998) Sequence-selective evaluation of peptide side-chain interaction. New artificial receptors for selective recognition in water. Journal of the American Chemical Society, 120, 11208-11209;
    • (1998) Journal of the American Chemical Society , vol.120 , pp. 11208-11209
    • Hossain, M.A.1    Schneider, H.J.2
  • 34
    • 0033591371 scopus 로고    scopus 로고
    • Porphyrin derivatives as water-soluble receptors for peptides
    • (b) Sirish M, Schneider HJ. (1999) Porphyrin derivatives as water-soluble receptors for peptides. Chemical Communications, 907-908. (Pubitemid 29248471)
    • (1999) Chemical Communications , Issue.10 , pp. 907-908
    • Sirish, M.1    Schneider, H.-J.2
  • 35
    • 34249275290 scopus 로고    scopus 로고
    • Effects of cucurbit[7]uril on enzymatic activity
    • DOI 10.1039/b618703j
    • Hennig A, Ghale G, Nau WM. (2007) Effects of cucurbit[7]uril on enzymatic activity. Chemical Communications, 1614-1616. (Pubitemid 46813947)
    • (2007) Chemical Communications , Issue.16 , pp. 1614-1616
    • Hennig, A.1    Ghale, G.2    Nau, W.M.3
  • 37
    • 77950272929 scopus 로고    scopus 로고
    • Supramolecular capsules: Under control
    • (b) Nau WM. (2010) Supramolecular capsules: under control. Nature Chemistry, 2, 248-250;
    • (2010) Nature Chemistry , vol.2 , pp. 248-250
    • Nau, W.M.1
  • 38
    • 48249090871 scopus 로고    scopus 로고
    • Salt-induced guest relocation from a macrocyclic cavity into a biomolecular pocket: Interplay between cucurbit[7]uril and albumin
    • (c) Shaikh M, Mohanty J, Bhasikuttan AC, Uzunova VD, Nau WM, Pal H. (2008) Salt-induced guest relocation from a macrocyclic cavity into a biomolecular pocket: interplay between cucurbit[7]uril and albumin. Chemical Communications, 3681-3683;
    • (2008) Chemical Communications , pp. 3681-3683
    • Shaikh, M.1    Mohanty, J.2    Bhasikuttan, A.C.3    Uzunova, V.D.4    Nau, W.M.5    Pal, H.6
  • 39
    • 80053135822 scopus 로고    scopus 로고
    • Strong binding of hydrocarbons to cucurbituril probed by fluorescent dye displacement: A supramolecular gas-sensing ensemble
    • (d) Florea M, Nau WM. (2011) Strong binding of hydrocarbons to cucurbituril probed by fluorescent dye displacement: a supramolecular gas-sensing ensemble. Angewandte Chemie International Edition, 50, 9338-9342.
    • (2011) Angewandte Chemie International Edition , vol.50 , pp. 9338-9342
    • Florea, M.1    Nau, W.M.2
  • 40
    • 70049089621 scopus 로고    scopus 로고
    • Favorable Effects of the Detergent and Enzyme Extraction Method for Preparing Decellularized Bovine Pericardium Scaffold for Tissue Engineered Heart Valves
    • (a) Yang M, Chen CZ, Wang XN, Zhu YB, Gu YJ. (2009) Favorable Effects of the Detergent and Enzyme Extraction Method for Preparing Decellularized Bovine Pericardium Scaffold for Tissue Engineered Heart Valves. Journal of Biomedical Materials Research Part B-Applied Biomaterials, 91B, 354-361;
    • (2009) Journal of Biomedical Materials Research Part B-Applied Biomaterials , vol.91 B , pp. 354-361
    • Yang, M.1    Chen, C.Z.2    Wang, X.N.3    Zhu, Y.B.4    Gu, Y.J.5
  • 41
    • 61449210913 scopus 로고    scopus 로고
    • A protocol for isolation and culture of mesenchymal stem cells from mouse bone marrow
    • (b) Soleimani M, Nadri S. (2009) A protocol for isolation and culture of mesenchymal stem cells from mouse bone marrow. Nature Protocols, 4, 102-106;
    • (2009) Nature Protocols , vol.4 , pp. 102-106
    • Soleimani, M.1    Nadri, S.2
  • 42
    • 65249149610 scopus 로고    scopus 로고
    • Designing protease sensors for real-time imaging of trypsin activation in pancreatic cancer cells
    • (c) Chen N, Zou J, Wang S, Ye Y, Huang Y, Gadda G, Yang JJ. (2009) Designing protease sensors for real-time imaging of trypsin activation in pancreatic cancer cells. Biochemistry, 48, 3519-3526;
    • (2009) Biochemistry , vol.48 , pp. 3519-3526
    • Chen, N.1    Zou, J.2    Wang, S.3    Ye, Y.4    Huang, Y.5    Gadda, G.6    Yang, J.J.7
  • 44
    • 0034651865 scopus 로고    scopus 로고
    • Proteases in the evaluation of pancreatic function and pancreatic disease
    • (e) Goldberg DM. (2000) Proteases in the evaluation of pancreatic function and pancreatic disease. Clinica Chimica Acta, 291, 201-221.
    • (2000) Clinica Chimica Acta , vol.291 , pp. 201-221
    • Goldberg, D.M.1
  • 45
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • DOI 10.1074/mcp.T400003-MCP200
    • Olsen JV, Ong SE, Mann M. (2004) Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Molecular & Cellular Proteomics, 3, 608-614. (Pubitemid 38878520)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.6 , pp. 608-614
    • Olsen, J.V.1    Ong, S.-E.2    Mann, M.3
  • 46
    • 0027479013 scopus 로고
    • Aminopeptidases: Structure and function
    • (a) Taylor A. (1993) Aminopeptidases: structure and function. FASEB Journal, 7, 290-298;
    • (1993) FASEB Journal , vol.7 , pp. 290-298
    • Taylor, A.1
  • 47
    • 33751550951 scopus 로고    scopus 로고
    • Leucine aminopeptidases: Diversity in structure and function
    • DOI 10.1515/BC.2006.191, PII BCHM387121535
    • (b) Matsui M, Fowler JH, Walling LL. (2006) Leucine aminopeptidases: diversity in structure and function. Biological Chemistry, 387, 1535-1544. (Pubitemid 44837577)
    • (2006) Biological Chemistry , vol.387 , Issue.12 , pp. 1535-1544
    • Matsui, M.1    Fowler, J.H.2    Walling, L.L.3
  • 48
    • 0035873704 scopus 로고    scopus 로고
    • 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide
    • (a) Cascio P, Hilton C, Kisselev AF, Rock KL, Goldberg AL. (2001) 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. The EMBO Journal, 20, 2357-2366;
    • (2001) The EMBO Journal , vol.20 , pp. 2357-2366
    • Cascio, P.1    Hilton, C.2    Kisselev, A.F.3    Rock, K.L.4    Goldberg, A.L.5
  • 49
    • 8744237281 scopus 로고    scopus 로고
    • Pathway for degradation of peptides generated by proteasomes: A key role for thimet oligopeptidase and other metallopeptidases
    • (b) Saric T, Graef CI, Goldberg AL. (2004) Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases. Journal of Biological Chemistry, 279, 46723-46732;
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 46723-46732
    • Saric, T.1    Graef, C.I.2    Goldberg, A.L.3
  • 50
    • 0347765874 scopus 로고    scopus 로고
    • Fluorescent probes for proteolysis: Tools for drug discovery
    • (c) Neefjes J, Dantuma NP. (2004) Fluorescent probes for proteolysis: tools for drug discovery. Nature Review Drug Discovery, 3, 58-69. (Pubitemid 38088698)
    • (2004) Nature Reviews Drug Discovery , vol.3 , Issue.1 , pp. 58-69
    • Neefjes, J.1    Dantuma, N.P.2
  • 51
    • 0344293603 scopus 로고
    • Leucine aminopeptidase in sequence determination of peptides
    • Hirs CHW, Timasheff SN (Ed.). Academic Press, New York
    • Light A. (1972) Leucine aminopeptidase in sequence determination of peptides. In Methods in Enzymology. Vol. 25, Hirs CHW, Timasheff SN (Ed.). Academic Press, New York, 253-262.
    • (1972) Methods in Enzymology , vol.25 , pp. 253-262
    • Light, A.1
  • 52
    • 84987421502 scopus 로고
    • Following enzyme catalysis in real-time inside a fast atom bombardment mass-spectrometer
    • Smith LA, Caprioli RM. (1983) Following enzyme catalysis in real-time inside a fast atom bombardment mass-spectrometer. Biomedical Mass Spectrometry, 10, 98-102.
    • (1983) Biomedical Mass Spectrometry , vol.10 , pp. 98-102
    • Smith, L.A.1    Caprioli, R.M.2
  • 54
    • 33748995918 scopus 로고    scopus 로고
    • Mass spectrometric real-time monitoring of enzymatic glycosidic hydrolysis, enzymatic inhibition and enzyme complexes
    • DOI 10.1007/s00216-006-0604-1
    • (b) Dennhart N, Letzel T. (2006) Mass spectrometric real-time monitoring of enzymatic glycosidic hydrolysis, enzymatic inhibition and enzyme complexes. Analytical and Bioanalytical Chemistry, 386, 689-698. (Pubitemid 44450952)
    • (2006) Analytical and Bioanalytical Chemistry , vol.386 , Issue.3 , pp. 689-698
    • Dennhart, N.1    Letzel, T.2
  • 58
    • 0014132705 scopus 로고
    • Preparation of Chemically Defined εN-Acetylated Trypsin
    • Labouess J, Gervais M. (1967) Preparation of Chemically Defined εN-Acetylated Trypsin. European Journal of Biochemistry, 2, 215-223.
    • (1967) European Journal of Biochemistry , vol.2 , pp. 215-223
    • Labouess, J.1    Gervais, M.2
  • 59
    • 0016807402 scopus 로고
    • Bovine Lens Leucine Aminopeptidase Number and State of Tryptophyl Residues
    • Misselwitz R, Zirwer D, Frohne M, Hanson H. (1975) Bovine Lens Leucine Aminopeptidase Number and State of Tryptophyl Residues. Febs Letters, 55, 233-236.
    • (1975) Febs Letters , vol.55 , pp. 233-236
    • Misselwitz, R.1    Zirwer, D.2    Frohne, M.3    Hanson, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.