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Volumn 117, Issue 1, 1998, Pages 255-261

Substrate specificity of barley cysteine endoproteases EP-A and EP-B

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOGENIC SUBSTRATE; CYSTEINE PROTEINASE; HORDEIN PROTEIN, HORDEUM VULGARE; VEGETABLE PROTEIN;

EID: 0032066103     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.117.1.255     Document Type: Article
Times cited : (48)

References (17)
  • 1
    • 0030091649 scopus 로고    scopus 로고
    • α-protected aminoacyl 7-amino-4-methyl-coumarin amide by phosphorus oxychloride and preparation of specific fluorogenic substrates for papain
    • α-protected aminoacyl 7-amino-4-methyl-coumarin amide by phosphorus oxychloride and preparation of specific fluorogenic substrates for papain. Peptide Res 9: 92-96
    • (1996) Peptide Res , vol.9 , pp. 92-96
    • Alves, L.C.1    Almeida, P.C.2    Franzoni, L.3    Juliano, L.4    Juliano, M.A.5
  • 2
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L
    • Barrett AJ, Kirschke H (1981) Cathepsin B, cathepsin H, and cathepsin L. Methods Enzymol C 80: 535-561
    • (1981) Methods Enzymol C , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 3
    • 0014942114 scopus 로고
    • Mapping the active site of papain with the aid of peptide substrates and inhibitors
    • Berger A, Schechter I (1970) Mapping the active site of papain with the aid of peptide substrates and inhibitors. Philos Trans R Soc Lond B 257: 249-264
    • (1970) Philos Trans R Soc Lond B , vol.257 , pp. 249-264
    • Berger, A.1    Schechter, I.2
  • 4
    • 0024155242 scopus 로고
    • Primary structure of a C-hordein gene from barley
    • Entwistle J (1988) Primary structure of a C-hordein gene from barley. Carlsberg Res Commun 53: 247-258
    • (1988) Carlsberg Res Commun , vol.53 , pp. 247-258
    • Entwistle, J.1
  • 5
    • 0022539027 scopus 로고
    • Peptide and protein molecular weight determination by electrophoresis using a high-molarity Tris buffer system without urea
    • Fling SP, Gregerson DS (1986) Peptide and protein molecular weight determination by electrophoresis using a high-molarity Tris buffer system without urea. Anal Biochem 155: 83-88
    • (1986) Anal Biochem , vol.155 , pp. 83-88
    • Fling, S.P.1    Gregerson, D.S.2
  • 6
    • 0026503894 scopus 로고
    • New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain
    • García-Echeverría C, Rich DH (1992a) New intramolecularly quenched fluorogenic peptide substrates for the study of the kinetic specificity of papain. FEBS Lett 297: 100-102
    • (1992) FEBS Lett , vol.297 , pp. 100-102
    • García-Echeverría, C.1    Rich, D.H.2
  • 7
    • 0026808963 scopus 로고
    • Effect of P2′ substituants on kinetic constants for hydrolysis by cysteine proteinases
    • García-Echeverría C, Rich DH (1992b) Effect of P2′ substituants on kinetic constants for hydrolysis by cysteine proteinases. Biochem Biophys Res Commun 187: 615-619
    • (1992) Biochem Biophys Res Commun , vol.187 , pp. 615-619
    • García-Echeverría, C.1    Rich, D.H.2
  • 9
    • 0001876687 scopus 로고
    • Release arid activation of barley beta-amylase by malt endopeptidases
    • Guerin JR, Lance RCM, Wallace W (1992) Release arid activation of barley beta-amylase by malt endopeptidases. J Cereal Sci 15: 5-14
    • (1992) J Cereal Sci , vol.15 , pp. 5-14
    • Guerin, J.R.1    Lance, R.C.M.2    Wallace, W.3
  • 11
    • 0026794955 scopus 로고
    • Small-angle x-ray-scattering studies of the C hordeins of barley (Hordeum vulgare)
    • I'Anson KJ, Morris VJ, Shewry PR, Tatham AS (1992) Small-angle x-ray-scattering studies of the C hordeins of barley (Hordeum vulgare). Biochem J 287: 183-185
    • (1992) Biochem J , vol.287 , pp. 183-185
    • I'Anson, K.J.1    Morris, V.J.2    Shewry, P.R.3    Tatham, A.S.4
  • 13
    • 0000587659 scopus 로고
    • A cysteine endopeptidase from barley malt which degrades hordein
    • Phillips HA, Wallace W (1989) A cysteine endopeptidase from barley malt which degrades hordein. Phytochemistry 28: 3285-3290
    • (1989) Phytochemistry , vol.28 , pp. 3285-3290
    • Phillips, H.A.1    Wallace, W.2
  • 14
    • 0000054574 scopus 로고
    • A proteinase from germinated barley. I. Purification and some physical properties of a 30-kD cysteine endoproteinase from green malt
    • Poulie M, Jones BL (1988) A proteinase from germinated barley. I. Purification and some physical properties of a 30-kD cysteine endoproteinase from green malt. Plant Physiol 88: 1454-1460
    • (1988) Plant Physiol , vol.88 , pp. 1454-1460
    • Poulie, M.1    Jones, B.L.2
  • 15
    • 0001864307 scopus 로고    scopus 로고
    • Studies on the activation and release of bound limit dextrinase in malted barley
    • Sissons MJ (1996) Studies on the activation and release of bound limit dextrinase in malted barley. J Am Soc Brew Chem 54: 19-25
    • (1996) J Am Soc Brew Chem , vol.54 , pp. 19-25
    • Sissons, M.J.1
  • 17
    • 0029849518 scopus 로고    scopus 로고
    • Purification and partial characterization of a 31-kDa cysteine endopeptidase from germinated barley
    • Zhang N, Jones BL (1996) Purification and partial characterization of a 31-kDa cysteine endopeptidase from germinated barley. Planta 199: 565-572
    • (1996) Planta , vol.199 , pp. 565-572
    • Zhang, N.1    Jones, B.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.