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Volumn 7, Issue 7, 2012, Pages

Biochemical and physical characterisation of urinary nanovesicles following CHAPS treatment

Author keywords

[No Author keywords available]

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; DIPEPTIDYL PEPTIDASE IV; DITHIOTHREITOL; NEPHRILYSIN; PROTEINASE; TAMM HORSFALL GLYCOPROTEIN; UNCLASSIFIED DRUG;

EID: 84863740390     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0037279     Document Type: Article
Times cited : (76)

References (60)
  • 2
  • 3
    • 4444226979 scopus 로고    scopus 로고
    • Identification and proteomic profiling of exosomes in human urine
    • Pisitkun T, Shen RF, Knepper MA, (2004) Identification and proteomic profiling of exosomes in human urine. Proc Natl Acad Sci U S A. 101: 13368-13373.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13368-13373
    • Pisitkun, T.1    Shen, R.F.2    Knepper, M.A.3
  • 7
    • 60549099598 scopus 로고    scopus 로고
    • Can urinary exosomes act as treatment response markers in prostate cancer?
    • Mitchell PJ, Welton J, Staffurth J, Court J, Mason MD, et al. (2009) Can urinary exosomes act as treatment response markers in prostate cancer? J Transl Med 7: 4-17.
    • (2009) J Transl Med , vol.7 , pp. 4-17
    • Mitchell, P.J.1    Welton, J.2    Staffurth, J.3    Court, J.4    Mason, M.D.5
  • 8
    • 49749121101 scopus 로고    scopus 로고
    • Urinary exosomal transcription factors, a new class of biomarkers for renal disease
    • Zhou H, Cheruvanky A, Hu X, Matsumoto T, Hiramatsu N, et al. (2008) Urinary exosomal transcription factors, a new class of biomarkers for renal disease. Kidney Int 74: 613-621.
    • (2008) Kidney Int , vol.74 , pp. 613-621
    • Zhou, H.1    Cheruvanky, A.2    Hu, X.3    Matsumoto, T.4    Hiramatsu, N.5
  • 9
    • 77954244728 scopus 로고    scopus 로고
    • Nucleic acids within urinary exosomes/microvesicles are potential biomarkers for renal disease Kidney Int
    • Miranda KC, Bond DT, McKee M, Skog J, Pǎunescu TG, et al. (2010) Nucleic acids within urinary exosomes/microvesicles are potential biomarkers for renal disease Kidney Int 78: 191-199.
    • (2010) , vol.78 , pp. 191-199
    • Miranda, K.C.1    Bond, D.T.2    McKee, M.3    Skog, J.4    Pǎunescu, T.G.5
  • 11
    • 19444385174 scopus 로고    scopus 로고
    • LDL receptor family: isolation, production, and ligand binding analysis
    • Bajari TM, Strasser V, Nimpf J, Schneider WJ, (2005) LDL receptor family: isolation, production, and ligand binding analysis. Methods 36: 109-16.
    • (2005) Methods , vol.36 , pp. 109-116
    • Bajari, T.M.1    Strasser, V.2    Nimpf, J.3    Schneider, W.J.4
  • 12
    • 0035298519 scopus 로고    scopus 로고
    • Conditions for solubilisation of Tamm-Horsfall protein/uromodulin in human urine and establishment of a sensitive and accurate enzyme-linked immunosorbent assay (ELISA) method
    • Kobayashi K, Fukuoka S, (2001) Conditions for solubilisation of Tamm-Horsfall protein/uromodulin in human urine and establishment of a sensitive and accurate enzyme-linked immunosorbent assay (ELISA) method. Archives of Biochemistry and Biophysics 388: 113-120.
    • (2001) Archives of Biochemistry and Biophysics , vol.388 , pp. 113-120
    • Kobayashi, K.1    Fukuoka, S.2
  • 13
    • 0346219110 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer
    • Busek P, Malík R, Sedo A, (2004) Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer. Int J Biochem Cell Biol 36: 408-421.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 408-421
    • Busek, P.1    Malík, R.2    Sedo, A.3
  • 14
    • 0024538318 scopus 로고
    • Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones
    • Erdos EG, Skidgel RA, (1989) Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J 3: 145-151.
    • (1989) FASEB J , vol.3 , pp. 145-151
    • Erdos, E.G.1    Skidgel, R.A.2
  • 16
    • 0013924036 scopus 로고
    • Factors determining the aggregation of urinary mucoprotein
    • McQueen EG, Engel EG, (1966) Factors determining the aggregation of urinary mucoprotein. J Clin Path 19: 392-396.
    • (1966) J Clin Path , vol.19 , pp. 392-396
    • McQueen, E.G.1    Engel, E.G.2
  • 18
    • 77956255640 scopus 로고    scopus 로고
    • Podocyte membrane vesicles in urine originate from tip vesiculation of podocyte microvilli
    • Hara M, Yanagihara T, Hirayama Y, Ogasawara S, Kurosawa H, et al. (2010) Podocyte membrane vesicles in urine originate from tip vesiculation of podocyte microvilli. Hum Pathol 41: 12665-1275.
    • (2010) Hum Pathol , vol.41 , pp. 11275-12665
    • Hara, M.1    Yanagihara, T.2    Hirayama, Y.3    Ogasawara, S.4    Kurosawa, H.5
  • 19
    • 0141528466 scopus 로고    scopus 로고
    • Characterisation of the biosynthesis and processing of the neutrophil granule membrane protein CD63 in myeloid cells
    • Agerberg M, Lindmark A, (2003) Characterisation of the biosynthesis and processing of the neutrophil granule membrane protein CD63 in myeloid cells. Clin Lab Haem 25: 297-306.
    • (2003) Clin Lab Haem , vol.25 , pp. 297-306
    • Agerberg, M.1    Lindmark, A.2
  • 20
    • 0038054203 scopus 로고    scopus 로고
    • Differential post-translational modification of CD63 molecules during maturation of human dendritic cells. Eur
    • Engering A, Kuhn L, Fluitsma D, Hoefsmit E, Pieters J, (2003) Differential post-translational modification of CD63 molecules during maturation of human dendritic cells. Eur. J. Biochem 270: 2412-2420.
    • (2003) J. Biochem , vol.270 , pp. 2412-2420
    • Engering, A.1    Kuhn, L.2    Fluitsma, D.3    Hoefsmit, E.4    Pieters, J.5
  • 22
    • 18344410673 scopus 로고    scopus 로고
    • Nephrinuria in diabetic nephropathy of type I diabetes
    • Patari A, Forsblom C, Havana M, Taipale H, Groop PH, et al. (2003) Nephrinuria in diabetic nephropathy of type I diabetes. Diabetes 52: 2969-2974.
    • (2003) Diabetes , vol.52 , pp. 2969-2974
    • Patari, A.1    Forsblom, C.2    Havana, M.3    Taipale, H.4    Groop, P.H.5
  • 23
    • 70350746686 scopus 로고    scopus 로고
    • Urine proteomics for profiling of human disease using high accuracy mass spectrometry
    • Kentsis A, Monigatti F, Dorff K, Campagne F, Bachur R, et al. (2009) Urine proteomics for profiling of human disease using high accuracy mass spectrometry. Proteomics Clin Appl 3: 1062-1071.
    • (2009) Proteomics Clin Appl , vol.3 , pp. 1062-1071
    • Kentsis, A.1    Monigatti, F.2    Dorff, K.3    Campagne, F.4    Bachur, R.5
  • 24
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • Adachi J, Kumar C, Zhang Y, Olsen JV, Mann M, (2006) The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. Genome Biol 7: R80.
    • (2006) Genome Biol , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 26
    • 70350449455 scopus 로고    scopus 로고
    • ExoCarta: A compendium of exosomal proteins and RNA
    • Mathivanan S, Simpson RJ, (2009) ExoCarta: A compendium of exosomal proteins and RNA. Proteomics 9: 4997-5000.
    • (2009) Proteomics , vol.9 , pp. 4997-5000
    • Mathivanan, S.1    Simpson, R.J.2
  • 27
    • 0141742293 scopus 로고    scopus 로고
    • PANTHER: a library of protein families and subfamilies indexed by function
    • Thomas PD, Campbell MJ, Kejariwal A, Mi H, Karlak B, et al. (2003) PANTHER: a library of protein families and subfamilies indexed by function. GenomeRes 13: 2129-2141.
    • (2003) GenomeRes , vol.13 , pp. 2129-2141
    • Thomas, P.D.1    Campbell, M.J.2    Kejariwal, A.3    Mi, H.4    Karlak, B.5
  • 29
    • 0002970919 scopus 로고
    • A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses
    • Tamm I, Horsfall FL Jr, (1952) A mucoprotein derived from human urine which reacts with influenza, mumps, and Newcastle disease viruses. J Exp Med 95: 71-97.
    • (1952) J Exp Med , vol.95 , pp. 71-97
    • Tamm, I.1    Horsfall Jr., F.L.2
  • 30
    • 0022361574 scopus 로고
    • A system for accurate immunolocalization of Tamm-Horsfall protein in renal biopsies
    • Kumar S, Jasani B, Hunt JS, Moffat DB, Asscher AW, (1985) A system for accurate immunolocalization of Tamm-Horsfall protein in renal biopsies. Histochem J 17: 1251-1258.
    • (1985) Histochem J , vol.17 , pp. 1251-1258
    • Kumar, S.1    Jasani, B.2    Hunt, J.S.3    Moffat, D.B.4    Asscher, A.W.5
  • 31
    • 0026445760 scopus 로고
    • The Asn-linked carbohydrate chains of human Tamm-Horsfall glycoprotein of one male. Novel sulphated and novel N-acetylgalactosamine-containing N-linked carbohydrate chains
    • Hard K, Van Zadelhoff G, Moonen P, Kamerling JP, Vliegenthart FG, (1992) The Asn-linked carbohydrate chains of human Tamm-Horsfall glycoprotein of one male. Novel sulphated and novel N-acetylgalactosamine-containing N-linked carbohydrate chains. Eur J Biochem 209: 895-915.
    • (1992) Eur J Biochem , vol.209 , pp. 895-915
    • Hard, K.1    van Zadelhoff, G.2    Moonen, P.3    Kamerling, J.P.4    Vliegenthart, F.G.5
  • 32
    • 0019761370 scopus 로고
    • Tamm- Horsfall uromucoprotein and the pathogenesis of casts, reflux nephropathy, and nephritides
    • Wenk RE, Bhagavan BS, Rudert J, (1981) Tamm- Horsfall uromucoprotein and the pathogenesis of casts, reflux nephropathy, and nephritides. Pathobiol Annu 11: 229-257.
    • (1981) Pathobiol Annu , vol.11 , pp. 229-257
    • Wenk, R.E.1    Bhagavan, B.S.2    Rudert, J.3
  • 33
    • 0021080229 scopus 로고
    • Protein composition of urinary casts from healthy subjects and patients with glomerulonephritis
    • Fairley JK, Owen JE, Birch DF, (1983) Protein composition of urinary casts from healthy subjects and patients with glomerulonephritis. Br Med J 287: 1838-1840.
    • (1983) Br Med J , vol.287 , pp. 1838-1840
    • Fairley, J.K.1    Owen, J.E.2    Birch, D.F.3
  • 35
    • 84856390943 scopus 로고    scopus 로고
    • Nanoparticles isolated from blood: a reflection of vesiculability of blood cells during the isolation process
    • Suštar V, Bedina-Zavec A, Stukelj R, et al. (2011) Nanoparticles isolated from blood: a reflection of vesiculability of blood cells during the isolation process. Int J Nanomedicine 6: 2737-2748.
    • (2011) Int J Nanomedicine , vol.6 , pp. 2737-2748
    • Suštar, V.1    Bedina-Zavec, A.2    Stukelj, R.3
  • 36
    • 0036307181 scopus 로고    scopus 로고
    • The ZP domain is a conserved module for polymerization of extracellular proteins
    • Jovine L, Qi H, Williams Z, Litscher E, Wassarman M, (2002) The ZP domain is a conserved module for polymerization of extracellular proteins. Nat Cell Biol 4: 457-461.
    • (2002) Nat Cell Biol , vol.4 , pp. 457-461
    • Jovine, L.1    Qi, H.2    Williams, Z.3    Litscher, E.4    Wassarman, M.5
  • 37
    • 0019082582 scopus 로고
    • A nondenaturing zwitterionic detergent for membrane biochemistry: design and synthesis
    • Hjelmeland LM, (1980) A nondenaturing zwitterionic detergent for membrane biochemistry: design and synthesis. Proc Natl Acad Sci USA 77: 6368-6370.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6368-6370
    • Hjelmeland, L.M.1
  • 38
    • 0023726480 scopus 로고
    • Solubilisation effect of Nonidet P-40, triton X-100 and CHAPS in the detection of MHC-like glycoproteins
    • Labeta MO, Fernandez N, Festenstein H, (1988) Solubilisation effect of Nonidet P-40, triton X-100 and CHAPS in the detection of MHC-like glycoproteins. J Immunol Methods 112: 133-138.
    • (1988) J Immunol Methods , vol.112 , pp. 133-138
    • Labeta, M.O.1    Fernandez, N.2    Festenstein, H.3
  • 39
    • 24044439517 scopus 로고    scopus 로고
    • Protein-protein interactions in the tetraspanin web
    • Levy S, Shoham T, (2005) Protein-protein interactions in the tetraspanin web. Physiology. 20: 218-224.
    • (2005) Physiology , vol.20 , pp. 218-224
    • Levy, S.1    Shoham, T.2
  • 41
    • 34247872835 scopus 로고    scopus 로고
    • Rapid isolation of urinary exosomal biomarkers using a nanomembrane ultrafiltration concentrator
    • Cheruvanky A, Zhou H, Pisitkun T, Kopp JB, Knepper MA, et al. (2007) Rapid isolation of urinary exosomal biomarkers using a nanomembrane ultrafiltration concentrator. Am J Physiol Renal Physiol 292: 1657-1661.
    • (2007) Am J Physiol Renal Physiol , vol.292 , pp. 1657-1661
    • Cheruvanky, A.1    Zhou, H.2    Pisitkun, T.3    Kopp, J.B.4    Knepper, M.A.5
  • 42
    • 77957557995 scopus 로고    scopus 로고
    • Comparison of three methods for isolation of urinary microvesicles to identify biomarkers of nephrotic syndrome
    • Rood IL, Deegens JK, Merchant ML, Tamboer WP, Wilkey DW, et al. (2010) Comparison of three methods for isolation of urinary microvesicles to identify biomarkers of nephrotic syndrome. Kidney Int 78: 810-816.
    • (2010) Kidney Int , vol.78 , pp. 810-816
    • Rood, I.L.1    de egens, J.K.2    Merchant, M.L.3    Tamboer, W.P.4    Wilkey, D.W.5
  • 43
    • 38949168914 scopus 로고    scopus 로고
    • Visualization of Detergent Solubilization of Membranes: Implications for the Isolation of Rafts
    • Garner AE, Smith DA, Hooper NM, (2008) Visualization of Detergent Solubilization of Membranes: Implications for the Isolation of Rafts. Biophysical J 94: 1326-1340.
    • (2008) Biophysical J , vol.94 , pp. 1326-1340
    • Garner, A.E.1    Smith, D.A.2    Hooper, N.M.3
  • 44
    • 0025779323 scopus 로고
    • Molecular cloning and primary structure of KELL blood group protein
    • Lee S, Zambas ED, Marsh WL, Redman CM, (1991) Molecular cloning and primary structure of KELL blood group protein. Proc Natl Acad Sci USA 88: 6353-6357.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 6353-6357
    • Lee, S.1    Zambas, E.D.2    Marsh, W.L.3    Redman, C.M.4
  • 45
    • 0028261084 scopus 로고
    • Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells
    • Shimada K, Takahashi M, Tanzawa K, (1994) Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J Biol Chem 269: 18275-18278.
    • (1994) J Biol Chem , vol.269 , pp. 18275-18278
    • Shimada, K.1    Takahashi, M.2    Tanzawa, K.3
  • 46
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane bound, phosphoramidon- sensitive metalloprotease with acidic pH optimum
    • Emoto N, Yanagisawa M, (1995) Endothelin-converting enzyme-2 is a membrane bound, phosphoramidon- sensitive metalloprotease with acidic pH optimum. J Biol Chem 270: 15262-15268.
    • (1995) J Biol Chem , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 47
    • 0034108631 scopus 로고    scopus 로고
    • The tetraspanin CD63/Lamp3 cycles between endocytic and secretory compartments in human endothelial cells. Mo
    • Kobayashi T, Vischer UM, Rosnoblet C, Lebrand C, Lindsey M, et al. (2000) The tetraspanin CD63/Lamp3 cycles between endocytic and secretory compartments in human endothelial cells. Mo. Biol Cell 11: 1829-1843.
    • (2000) Biol Cell , vol.11 , pp. 1829-1843
    • Kobayashi, T.1    Vischer, U.M.2    Rosnoblet, C.3    Lebrand, C.4    Lindsey, M.5
  • 48
    • 0035877018 scopus 로고    scopus 로고
    • Proteomic analysis of dendritic cell-derived exosomes a secreted subcellular compartement distinct from apoptotic vesicles
    • Thery C, Boussac M, Veron P, Ricciardi-Castagnoli P, Raposo G, et al. (2001) Proteomic analysis of dendritic cell-derived exosomes a secreted subcellular compartement distinct from apoptotic vesicles. J. Immunol 166: 7309-7318.
    • (2001) J. Immunol , vol.166 , pp. 7309-7318
    • Thery, C.1    Boussac, M.2    Veron, P.3    Ricciardi-Castagnoli, P.4    Raposo, G.5
  • 49
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst M, Odorizzi G, Estepa EJ, Emr SD, (2000) Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 1: 248-258.
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 50
    • 58149517753 scopus 로고    scopus 로고
    • Exosomes Packing APOBEC3G confer human immunodeficiency virus resistance to recipient cells
    • Khatua AK, TaylorHE, Hildreth JE, Popik W, (2009) Exosomes Packing APOBEC3G confer human immunodeficiency virus resistance to recipient cells. J Virol 83: 512-521.
    • (2009) J Virol , vol.83 , pp. 512-521
    • Khatua, A.K.1    Taylor, H.E.2    Hildreth, J.E.3    Popik, W.4
  • 51
    • 66149128052 scopus 로고    scopus 로고
    • SED1/MFG-E8 a bi-motif protein that orchestrates diverse cellular interactions
    • Raymond A, Ensslin MA, Shur BD, (2009) SED1/MFG-E8 a bi-motif protein that orchestrates diverse cellular interactions. J Cell Biochem 106: 957-66.
    • (2009) J Cell Biochem , vol.106 , pp. 957-966
    • Raymond, A.1    Ensslin, M.A.2    Shur, B.D.3
  • 52
    • 0036178402 scopus 로고    scopus 로고
    • Secretion of a peripheral membrane protein, MFG-E8, as a complex with membrane vesicles
    • Oshima K, Aoki N, Kato T, Kitajima K, Matsuda T, (2002) Secretion of a peripheral membrane protein, MFG-E8, as a complex with membrane vesicles. Eur J Biochem 269: 1209-1218.
    • (2002) Eur J Biochem , vol.269 , pp. 1209-1218
    • Oshima, K.1    Aoki, N.2    Kato, T.3    Kitajima, K.4    Matsuda, T.5
  • 53
    • 0043029287 scopus 로고    scopus 로고
    • Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding
    • Ensslin MA, Shur BD, (2003) Identification of mouse sperm SED1, a bimotif EGF repeat and discoidin-domain protein involved in sperm-egg binding. Cell 114: 405-417.
    • (2003) Cell , vol.114 , pp. 405-417
    • Ensslin, M.A.1    Shur, B.D.2
  • 54
    • 23744458517 scopus 로고    scopus 로고
    • Production of the long and short forms of MGF-E8 by epidermal keratinocytes
    • Watanabe T, Totsuka R, Miyatani S, Kurata S, Sato S, et al. (2005) Production of the long and short forms of MGF-E8 by epidermal keratinocytes. Cell Tissue Res 321: 185-193.
    • (2005) Cell Tissue Res , vol.321 , pp. 185-193
    • Watanabe, T.1    Totsuka, R.2    Miyatani, S.3    Kurata, S.4    Sato, S.5
  • 55
    • 24644447311 scopus 로고    scopus 로고
    • Accumulation of MFG-E8/lactadherin on exosomes from immature dendritic cells
    • Veron P, Segura E, Sugano G, Amigorena S, Thery C, (2005) Accumulation of MFG-E8/lactadherin on exosomes from immature dendritic cells. Blood Cells Mol Dis 35: 81-88.
    • (2005) Blood Cells Mol Dis , vol.35 , pp. 81-88
    • Veron, P.1    Segura, E.2    Sugano, G.3    Amigorena, S.4    Thery, C.5
  • 56
    • 18344410673 scopus 로고    scopus 로고
    • Nephrinuria in diabetic nephropathy of type I diabetes
    • Patari A, Forsblom C, Havana M, Taipale H, Groop PH, et al. (2003) Nephrinuria in diabetic nephropathy of type I diabetes. Diabetes 52: 2969-2974.
    • (2003) Diabetes , vol.52 , pp. 2969-2974
    • Patari, A.1    Forsblom, C.2    Havana, M.3    Taipale, H.4    Groop, P.H.5
  • 57
    • 20544440811 scopus 로고    scopus 로고
    • Apical cell membranes are shed into urine from injured podocytes: a novel phenomenon of podocyte injury
    • Hara M, Yanagihara T, Kihara I, Higashi K, Fujimoto K, et al. (2005) Apical cell membranes are shed into urine from injured podocytes: a novel phenomenon of podocyte injury. J Am Soc Nephrol 16: 408-16.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 408-416
    • Hara, M.1    Yanagihara, T.2    Kihara, I.3    Higashi, K.4    Fujimoto, K.5
  • 59
    • 0028936353 scopus 로고
    • Progesterone-induced secretion of dypeptidyl peptidase-IV (cluster differentiation antigen-26) by the uterine endometrium of the ewe and cow that costimulates lymphocyte proliferation
    • Liu WJ, Hansen PJ, (1995) Progesterone-induced secretion of dypeptidyl peptidase-IV (cluster differentiation antigen-26) by the uterine endometrium of the ewe and cow that costimulates lymphocyte proliferation. Endocrinology 136: 779-87.
    • (1995) Endocrinology , vol.136 , pp. 779-787
    • Liu, W.J.1    Hansen, P.J.2
  • 60
    • 0021137049 scopus 로고
    • A highly sensitive fluorimetric assay for "enkephalinase",a neutral metalloendopeptidase that releases Tyr-Gly- Gly from enkephalins
    • Florentin D, Sassi A, Roques BP, (1984) A highly sensitive fluorimetric assay for "enkephalinase" Anal Biochem 141: 62-69 a neutral metalloendopeptidase that releases Tyr-Gly- Gly from enkephalins.
    • (1984) Anal Biochem , vol.141 , pp. 62-69
    • Florentin, D.1    Sassi, A.2    Roques, B.P.3


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