메뉴 건너뛰기




Volumn 119, Issue 4, 1999, Pages 1261-1269

Molecular cloning and characterization of apricot fruit polyphenol oxidase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID ANALYSIS; CATECHOL OXIDASE; CDNA LIBRARY; DNA PROBE; MOLECULAR CLONING; MOLECULAR GENETICS; MULTIGENE FAMILY; OPEN READING FRAME; PLANT PRODUCT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

EID: 0033117525     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.119.4.1261     Document Type: Article
Times cited : (73)

References (44)
  • 2
    • 0001741062 scopus 로고
    • Genetics of actin-related sequences in tomato
    • Bernatzky R, Tanksley SD (1986) Genetics of actin-related sequences in tomato. Theor Appl Genet 72: 314-321
    • (1986) Theor Appl Genet , vol.72 , pp. 314-321
    • Bernatzky, R.1    Tanksley, S.D.2
  • 3
    • 0029159295 scopus 로고
    • An apple polyphenol oxidase cDNA is up-regulated in wounded tissues
    • Boss PK, Gardner RC, Janssen B-J, Ross GS (1995) An apple polyphenol oxidase cDNA is up-regulated in wounded tissues. Plant Mol Biol 27: 429-433
    • (1995) Plant Mol Biol , vol.27 , pp. 429-433
    • Boss, P.K.1    Gardner, R.C.2    Janssen, B.-J.3    Ross, G.S.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0026930134 scopus 로고
    • Cloning and characterization of a cDNA coding for Vicia faba polyphenoloxidase
    • Cary JW, Lax AR, Flurkey WH (1992) Cloning and characterization of a cDNA coding for Vicia faba polyphenoloxidase. Plant Mol Biol 20: 245-253
    • (1992) Plant Mol Biol , vol.20 , pp. 245-253
    • Cary, J.W.1    Lax, A.R.2    Flurkey, W.H.3
  • 6
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F (1988) Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res 16 (22): 10881-10890
    • (1988) Nucleic Acids Res , vol.16 , Issue.22 , pp. 10881-10890
    • Corpet, F.1
  • 7
    • 0026047161 scopus 로고
    • Chloroplast protein topogenesis: Import, sorting, and assembly
    • De Boer AD, Weisbeek PJ (1991) Chloroplast protein topogenesis: import, sorting, and assembly. Biochim Biophys Acta 1071: 221-253
    • (1991) Biochim Biophys Acta , vol.1071 , pp. 221-253
    • De Boer, A.D.1    Weisbeek, P.J.2
  • 8
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P, Smithies O (1984) A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-395
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 9
    • 0028519224 scopus 로고
    • Molecular cloning and characterisation of grape berry polyphenoloxidase
    • Dry IB, Robinson SP (1994) Molecular cloning and characterisation of grape berry polyphenoloxidase. Plant Mol Biol 26: 495-502
    • (1994) Plant Mol Biol , vol.26 , pp. 495-502
    • Dry, I.B.1    Robinson, S.P.2
  • 10
    • 0000856441 scopus 로고
    • Enzymatic antinutritive defenses of the tomato plant against insects
    • P Hedin, ed American Chemical Society, Washington, DC
    • Duffey S, Felton G (1991) Enzymatic antinutritive defenses of the tomato plant against insects. In P Hedin, ed, Naturally Occurring Pest Bioregulators. American Chemical Society, Washington, DC, pp 166-197
    • (1991) Naturally Occurring Pest Bioregulators , pp. 166-197
    • Duffey, S.1    Felton, G.2
  • 11
    • 0000306322 scopus 로고
    • Tomato peroxidases. Purification and some properties
    • Fils B, Sauvage X, Nicolas J (1985) Tomato peroxidases. Purification and some properties. Sci Aliments 5: 217-232
    • (1985) Sci Aliments , vol.5 , pp. 217-232
    • Fils, B.1    Sauvage, X.2    Nicolas, J.3
  • 12
    • 0030138770 scopus 로고    scopus 로고
    • A cherry protein and its gene, abundantly expressed in ripening fruit, have been identified as thaumatin-like
    • Fils-Lycaon BR, Wiersma PA, Eastwell KC, Sautiere P (1996) A cherry protein and its gene, abundantly expressed in ripening fruit, have been identified as thaumatin-like. Plant Physiol 111: 269-273
    • (1996) Plant Physiol , vol.111 , pp. 269-273
    • Fils-Lycaon, B.R.1    Wiersma, P.A.2    Eastwell, K.C.3    Sautiere, P.4
  • 13
    • 0001088525 scopus 로고
    • Biochemical and immunochemical characteristics of polyphenol oxidases from different fruits of Prunus
    • Fraignier MP, Marques L, Fleuriet A, Macheix JJ (1995) Biochemical and immunochemical characteristics of polyphenol oxidases from different fruits of Prunus. J Agric Food Chem 43: 2375-2380
    • (1995) J Agric Food Chem , vol.43 , pp. 2375-2380
    • Fraignier, M.P.1    Marques, L.2    Fleuriet, A.3    Macheix, J.J.4
  • 14
    • 0030912625 scopus 로고    scopus 로고
    • Polyphenoloxidases from Williams pear (Pyrus communis L. cv williams): Activation, purification and some properties
    • Gauillard F, Richard-Forget F (1997) Polyphenoloxidases from Williams pear (Pyrus communis L. cv Williams): activation, purification and some properties. J Sci Food Agric 74: 49-56
    • (1997) J Sci Food Agric , vol.74 , pp. 49-56
    • Gauillard, F.1    Richard-Forget, F.2
  • 16
    • 0001012399 scopus 로고
    • Polyphenoloxidase from apple, partial purification, and some properties
    • Janovitz-Klapp A, Richard F, Nicolas J (1989) Polyphenoloxidase from apple, partial purification, and some properties. Phytochemistry 28: 2903-2907
    • (1989) Phytochemistry , vol.28 , pp. 2903-2907
    • Janovitz-Klapp, A.1    Richard, F.2    Nicolas, J.3
  • 17
    • 0023650367 scopus 로고
    • Putative polyadenylation signals in nuclear genes of higher plants: A compilation and analysis
    • Joshi CP (1987) Putative polyadenylation signals in nuclear genes of higher plants: a compilation and analysis. Nucleic Acids Res 15: 9627-9641
    • (1987) Nucleic Acids Res , vol.15 , pp. 9627-9641
    • Joshi, C.P.1
  • 18
    • 0029278837 scopus 로고
    • Cloning and characterization of polyphenol oxidase cDNAs of Phytolacca americana
    • Joy RW, Sugiyama M, Fukuda H, Komamine A (1995) Cloning and characterization of polyphenol oxidase cDNAs of Phytolacca americana. Plant Physiol 107: 1083-1089
    • (1995) Plant Physiol , vol.107 , pp. 1083-1089
    • Joy, R.W.1    Sugiyama, M.2    Fukuda, H.3    Komamine, A.4
  • 19
    • 84985201184 scopus 로고
    • Effects of proteins, protein hydrolyzates and amino acids on O-dihydroxyphenolase activity of polyphenol oxidase of mushroom, avocado and banana
    • Kahn V (1977) Effects of proteins, protein hydrolyzates and amino acids on O-dihydroxyphenolase activity of polyphenol oxidase of mushroom, avocado and banana. J Food Sci 50: 111-119
    • (1977) J Food Sci , vol.50 , pp. 111-119
    • Kahn, V.1
  • 20
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of protein
    • Kyte M, Doolittle RF (1982) A simple method for displaying the hydropathic character of protein. J Mol Biol 157: 105-132
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, M.1    Doolittle, R.F.2
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 49249153466 scopus 로고
    • Polyphenol oxidases in plants
    • Mayer AM, Harel E (1979) Polyphenol oxidases in plants. Phytochemistry 18: 193-215
    • (1979) Phytochemistry , vol.18 , pp. 193-215
    • Mayer, A.M.1    Harel, E.2
  • 24
    • 0001030216 scopus 로고
    • Phenoloxidases and their significance in fruit and vegetables
    • FP Fox, ed Elsevier Science Publishers, New York
    • Mayer AM, Harel E (1991) Phenoloxidases and their significance in fruit and vegetables. In FP Fox, ed, Food Enzymology. Elsevier Science Publishers, New York, pp 373-398
    • (1991) Food Enzymology , pp. 373-398
    • Mayer, A.M.1    Harel, E.2
  • 27
    • 0001623476 scopus 로고
    • Aberrant processing of polyphenol oxidase in a variegated grapevine mutant
    • Rathjen AH, Robinson SP (1992) Aberrant processing of polyphenol oxidase in a variegated grapevine mutant. Plant Physiol 99: 1619-1625
    • (1992) Plant Physiol , vol.99 , pp. 1619-1625
    • Rathjen, A.H.1    Robinson, S.P.2
  • 28
    • 0001235603 scopus 로고
    • Broad bean leaf polyphenol oxidase is a 60-kD protein susceptible to proteolytic cleavage
    • Robinson SP, Dry IB (1992) Broad bean leaf polyphenol oxidase is a 60-kD protein susceptible to proteolytic cleavage. Plant Physiol 99: 317-323
    • (1992) Plant Physiol , vol.99 , pp. 317-323
    • Robinson, S.P.1    Dry, I.B.2
  • 29
    • 0003040201 scopus 로고
    • Polyphenol oxidase enzymes in the sap and skin of mango fruit
    • Robinson SP, Loveys BR, Chacko EK (1993) Polyphenol oxidase enzymes in the sap and skin of mango fruit. J Plant Physiol 20: 99-107
    • (1993) J Plant Physiol , vol.20 , pp. 99-107
    • Robinson, S.P.1    Loveys, B.R.2    Chacko, E.K.3
  • 30
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia
    • Saiki RK, Scharf S, Faloona F, Mullis KB, Horn GT, Erlich H, Arnheim N (1985) Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science 230: 1350-1354
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.K.1    Scharf, S.2    Faloona, F.3    Mullis, K.B.4    Horn, G.T.5    Erlich, H.6    Arnheim, N.7
  • 32
    • 0000872610 scopus 로고
    • Substrate-dependent activation of latent potato leaf polyphenol oxidase by anionic surfactants
    • Sanchez-Ferrer A, Laveda F, Garcia-Carmona F (1993) Substrate-dependent activation of latent potato leaf polyphenol oxidase by anionic surfactants. J Agric Food Chem 41: 1583-1586
    • (1993) J Agric Food Chem , vol.41 , pp. 1583-1586
    • Sanchez-Ferrer, A.1    Laveda, F.2    Garcia-Carmona, F.3
  • 33
    • 0026812465 scopus 로고
    • The tomato 66.3-kD polyphenoloxidase gene: Molecular identification and developmental expression
    • Shahar T, Henning N, Gutfinger T, Hareven D, Lifschitz E (1992) The tomato 66.3-kD polyphenoloxidase gene: molecular identification and developmental expression. Plant Cell 4: 135-147
    • (1992) Plant Cell , vol.4 , pp. 135-147
    • Shahar, T.1    Henning, N.2    Gutfinger, T.3    Hareven, D.4    Lifschitz, E.5
  • 34
    • 0000894326 scopus 로고
    • Improved methods for the extraction of polyphenol oxidase from d'Anjou pears
    • Smith DM, Montgomery MW (1985) Improved methods for the extraction of polyphenol oxidase from d'Anjou pears. Phytochemistry 24: 901-904
    • (1985) Phytochemistry , vol.24 , pp. 901-904
    • Smith, D.M.1    Montgomery, M.W.2
  • 35
    • 0029137534 scopus 로고
    • Properties of carrot polyphenoloxidase
    • Söderhall I (1995) Properties of carrot polyphenoloxidase. Phytochemistry 39: 33-38
    • (1995) Phytochemistry , vol.39 , pp. 33-38
    • Söderhall, I.1
  • 36
    • 0028486184 scopus 로고
    • Import, targeting, and processing of a plant polyphenol oxidase
    • Sommer A, Nemann E, Steffens JC (1994) Import, targeting, and processing of a plant polyphenol oxidase. Plant Physiol 105: 1301-1311
    • (1994) Plant Physiol , vol.105 , pp. 1301-1311
    • Sommer, A.1    Nemann, E.2    Steffens, J.C.3
  • 37
    • 0029379574 scopus 로고
    • Polyphenol oxidase in potato. A multigene family that exhibits differential expression patterns
    • Thygesen PW, Dry IB, Robinson SP (1995) Polyphenol oxidase in potato. A multigene family that exhibits differential expression patterns. Plant Physiol 109: 525-531
    • (1995) Plant Physiol , vol.109 , pp. 525-531
    • Thygesen, P.W.1    Dry, I.B.2    Robinson, S.P.3
  • 38
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of protein from polyacrylamide gel to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 76: 4350-4354
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 39
    • 0002219004 scopus 로고
    • Polyphenol oxidase and photosynthesis research
    • Trebst A, Depka B (1995) Polyphenol oxidase and photosynthesis research. Photosynth Res 46: 41-44
    • (1995) Photosynth Res , vol.46 , pp. 41-44
    • Trebst, A.1    Depka, B.2
  • 40
    • 0031213675 scopus 로고    scopus 로고
    • Sequence and structural features of plant and fungal tyrosinases
    • Van Gelder CWG, Flurkey WH, Wichers HJ (1997) Sequence and structural features of plant and fungal tyrosinases. Phytochemistry 45: 1309-1323
    • (1997) Phytochemistry , vol.45 , pp. 1309-1323
    • Van Gelder, C.W.G.1    Flurkey, W.H.2    Wichers, H.J.3
  • 41
    • 84989742205 scopus 로고
    • Tentoxin stops the processing of polyphenol oxidase into an active protein
    • Vaughn KC, Duke SO (1984) Tentoxin stops the processing of polyphenol oxidase into an active protein. Physiol Plant 60: 257-261
    • (1984) Physiol Plant , vol.60 , pp. 257-261
    • Vaughn, K.C.1    Duke, S.O.2
  • 42
    • 0000975516 scopus 로고
    • Polyphenol oxidase: The chloroplast oxidase with no established function
    • Vaughn KC, Lax AR, Duke SO (1988) Polyphenol oxidase: the chloroplast oxidase with no established function. Physiol Plant 72: 659-665
    • (1988) Physiol Plant , vol.72 , pp. 659-665
    • Vaughn, K.C.1    Lax, A.R.2    Duke, S.O.3
  • 43
    • 0028072757 scopus 로고
    • A modified hot borate method significantly enhances the yield of high-quality RNA from cotton (Gossypium hirsutum l.)
    • Wan C-Y, Wilkins TA (1994) A modified hot borate method significantly enhances the yield of high-quality RNA from cotton (Gossypium hirsutum L.). Anal Biochem 223: 7-12
    • (1994) Anal Biochem , vol.223 , pp. 7-12
    • Wan, C.-Y.1    Wilkins, T.A.2
  • 44
    • 0000517995 scopus 로고
    • Polyphenol oxidase
    • DS Robinson, NAM Eskin, eds Elsevier Science Publishers, London
    • Zawistowski J, Biliaderis CG, Eskin NAM (1991) Polyphenol oxidase. In DS Robinson, NAM Eskin, eds, Oxidative Enzymes in Foods. Elsevier Science Publishers, London, pp 217-273
    • (1991) Oxidative Enzymes in Foods , pp. 217-273
    • Zawistowski, J.1    Biliaderis, C.G.2    Eskin, N.A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.