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Volumn 57, Issue 1, 2007, Pages 65-73

Manganese and molybdenum affect acid phosphatases from potatoes

Author keywords

Acid phosphatase origin; Buffers; Manganese; Molybdenum

Indexed keywords

IPOMOEA BATATAS; SOLANUM TUBEROSUM;

EID: 33847274686     PISSN: 09064710     EISSN: 16511913     Source Type: Journal    
DOI: 10.1080/09064710600641862     Document Type: Article
Times cited : (6)

References (33)
  • 1
    • 18744416823 scopus 로고    scopus 로고
    • Purification and characterization of two secreted purple acid phosphatase isozymes from phosphate-starved tomato (Lycopersicon esculentum) cell cultures
    • Bozzo, G., Raghothama, K., & Plaxton, W. (2002). Purification and characterization of two secreted purple acid phosphatase isozymes from phosphate-starved tomato (Lycopersicon esculentum) cell cultures. European Journal of Biochemistry, 269, 6278-6286.
    • (2002) European Journal of Biochemistry , vol.269 , pp. 6278-6286
    • Bozzo, G.1    Raghothama, K.2    Plaxton, W.3
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle protein-dye binding
    • Bradford, M. (1976). A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.1
  • 5
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum protein
    • Davis, B. (1964). Disc electrophoresis. II. Method and application to human serum protein. Annals of the New York Academy of Science, 121, 407-427.
    • (1964) Annals of the New York Academy of Science , vol.121 , pp. 407-427
    • Davis, B.1
  • 6
    • 0027950058 scopus 로고
    • The role of acid phosphatase in plant phosphorus metabolism
    • Duff, S.M., Sarat, G., & Plaxton, W. (1994). The role of acid phosphatase in plant phosphorus metabolism. Physiologia Plantarum, 90, 791-800.
    • (1994) Physiologia Plantarum , vol.90 , pp. 791-800
    • Duff, S.M.1    Sarat, G.2    Plaxton, W.3
  • 8
    • 0033559677 scopus 로고    scopus 로고
    • The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas): Metal content and spectroscopic characterization
    • Durmus, A., Eicken, C., Sift, B., Kratel, A., Kappl, R., Ergen, J., Hüttermann, H., & Krebs, B. (1999). The active site of purple acid phosphatase from sweet potatoes (Ipomoea batatas): metal content and spectroscopic characterization. European Journal of Biochemistry, 260, 709-716.
    • (1999) European Journal of Biochemistry , vol.260 , pp. 709-716
    • Durmus, A.1    Eicken, C.2    Sift, B.3    Kratel, A.4    Kappl, R.5    Ergen, J.6    Hüttermann, H.7    Krebs, B.8
  • 9
    • 0028005901 scopus 로고
    • Acid phosphatase activity in bean and cowpea plants grown under phosphorus stress
    • Fernández, D.S., & Ascencio, J. (1994). Acid phosphatase activity in bean and cowpea plants grown under phosphorus stress. Journal of Plant Nutrition, 17, 229-241.
    • (1994) Journal of Plant Nutrition , vol.17 , pp. 229-241
    • Fernández, D.S.1    Ascencio, J.2
  • 10
    • 0028140651 scopus 로고
    • Purification and characterization of potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity
    • Gellatly, K.S., Moorhead, G.B., Duff, S.M., Lefebvre, D.D., & Plaxton, W.C. (1994). Purification and characterization of potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity. Plant Physiology, 106, 223-232.
    • (1994) Plant Physiology , vol.106 , pp. 223-232
    • Gellatly, K.S.1    Moorhead, G.B.2    Duff, S.M.3    Lefebvre, D.D.4    Plaxton, W.C.5
  • 11
    • 77956758681 scopus 로고    scopus 로고
    • Gianfreda, L., Rao, M.A., Saccomandi, F., Sannino, F., & Violante, A. (2002). Enzymes in soil: properties, behaviour and potential applications. In A Violante, PM Huang, JM Bollag, L Gianfreda (Eds.), Soil mineral-organic mattermicroorganism interactions and ecosystem health. (pp. 301-328). Development in Soil Science 28B, London: Elsevier.
    • Gianfreda, L., Rao, M.A., Saccomandi, F., Sannino, F., & Violante, A. (2002). Enzymes in soil: properties, behaviour and potential applications. In A Violante, PM Huang, JM Bollag, L Gianfreda (Eds.), Soil mineral-organic mattermicroorganism interactions and ecosystem health. (pp. 301-328). Development in Soil Science 28B, London: Elsevier.
  • 12
    • 0032054250 scopus 로고    scopus 로고
    • Characterization of a cytosolic phosphatase from pea plumules having significant protein tyrosine phosphatase activity
    • Guo, Y., Terry, M.E., & Roux, S.J. (1998). Characterization of a cytosolic phosphatase from pea plumules having significant protein tyrosine phosphatase activity. Plant Physiology of Biochemistry, 36, 269-278.
    • (1998) Plant Physiology of Biochemistry , vol.36 , pp. 269-278
    • Guo, Y.1    Terry, M.E.2    Roux, S.J.3
  • 13
    • 0029903687 scopus 로고    scopus 로고
    • Partial purification and characterization of a type 1 protein phosphatase in purified nuclei of pea plumules
    • Guo, Y., & Roux, S.J. (1996). Partial purification and characterization of a type 1 protein phosphatase in purified nuclei of pea plumules. Biochemical Journal, 319, 985-991.
    • (1996) Biochemical Journal , vol.319 , pp. 985-991
    • Guo, Y.1    Roux, S.J.2
  • 14
    • 3042807068 scopus 로고    scopus 로고
    • Enzymes in organic media forms, functions and applications
    • Gupta, M.N., & Roy, I. (2004). Enzymes in organic media forms, functions and applications. European Journal of Biochemistry, 271, 2575-2583.
    • (2004) European Journal of Biochemistry , vol.271 , pp. 2575-2583
    • Gupta, M.N.1    Roy, I.2
  • 15
    • 33847278770 scopus 로고    scopus 로고
    • Horton, H.R., Moran, L.A., Ochs, R.S., Rawn, J.D., & Scrimgeour, K.G. (1993). V. Propiedades de las enzimas. In K Hodgin, & M Ryan (Eds.), Bioquimica (pp. 1-37). Prentice Hall Inc, México.
    • Horton, H.R., Moran, L.A., Ochs, R.S., Rawn, J.D., & Scrimgeour, K.G. (1993). V. Propiedades de las enzimas. In K Hodgin, & M Ryan (Eds.), Bioquimica (pp. 1-37). Prentice Hall Inc, México.
  • 16
    • 0034521412 scopus 로고    scopus 로고
    • Effects of copper on the kinetics of free and immobilized acid phosphatase
    • Huang, Q., & Shindo, H. (2000). Effects of copper on the kinetics of free and immobilized acid phosphatase. Soil Biology and Biochemistry, 32, 1885-1892.
    • (2000) Soil Biology and Biochemistry , vol.32 , pp. 1885-1892
    • Huang, Q.1    Shindo, H.2
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural protein during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 19
    • 0031802586 scopus 로고    scopus 로고
    • Kinetic properties and stability of potato acid phosphatase immobilized on Ca-polygalacturonate
    • Marzadori, C., Gessa, C., & Ciurli, S. (1998). Kinetic properties and stability of potato acid phosphatase immobilized on Ca-polygalacturonate. Biology and Fertility of Soils, 27, 97-103.
    • (1998) Biology and Fertility of Soils , vol.27 , pp. 97-103
    • Marzadori, C.1    Gessa, C.2    Ciurli, S.3
  • 20
    • 0013770438 scopus 로고
    • Studies on acid hydrolases in adult and foetal tissues. Acid rho-nitrophenyl phosphate phosphohydrolases of adult guinea-pig liver
    • Neil, M.W., & Horner, M.W. (1964). Studies on acid hydrolases in adult and foetal tissues. Acid rho-nitrophenyl phosphate phosphohydrolases of adult guinea-pig liver. Biochemical Journal, 92, 217-224.
    • (1964) Biochemical Journal , vol.92 , pp. 217-224
    • Neil, M.W.1    Horner, M.W.2
  • 21
    • 2342470541 scopus 로고    scopus 로고
    • Plant purple acid phosphatases: Genes, structures and biological function
    • Olczack, M., Morawiecka, B., & Watorek, W. (2003). Plant purple acid phosphatases: genes, structures and biological function. Acta Biochimimica Polonica, 50, 1245-1257.
    • (2003) Acta Biochimimica Polonica , vol.50 , pp. 1245-1257
    • Olczack, M.1    Morawiecka, B.2    Watorek, W.3
  • 22
    • 0030301302 scopus 로고    scopus 로고
    • Interaction of acid phosphatase with clays, organic molecules and organo-mineral complexes
    • Rao, M.A., Gianfreda, L., Palmiero, F., & Violante, A. (1996). Interaction of acid phosphatase with clays, organic molecules and organo-mineral complexes. Soil Science, 11, 751-760.
    • (1996) Soil Science , vol.11 , pp. 751-760
    • Rao, M.A.1    Gianfreda, L.2    Palmiero, F.3    Violante, A.4
  • 23
    • 0033923718 scopus 로고    scopus 로고
    • Interaction of acid phosphatase with clays, organic molecules and organomineral complexes: Kinetics and stability
    • Rao, M.A., Violante, A., & Gianfreda, L. (2000). Interaction of acid phosphatase with clays, organic molecules and organomineral complexes: kinetics and stability. Soil Biology and Biochemistry, 32, 1007-1014.
    • (2000) Soil Biology and Biochemistry , vol.32 , pp. 1007-1014
    • Rao, M.A.1    Violante, A.2    Gianfreda, L.3
  • 24
    • 0034058387 scopus 로고    scopus 로고
    • On the salt-induced activation of lyophilized enzymes in organic solvents: Effect of salt kosmotropicity on enzyme activity
    • Ru, M.T., Hirokane, S.Y., Lo, A.S., Dordick, J.S., Reimer, J.A., & Clark, D.S. (2000). On the salt-induced activation of lyophilized enzymes in organic solvents: effect of salt kosmotropicity on enzyme activity. Journal of American Chemical Society, 122, 1565-1571.
    • (2000) Journal of American Chemical Society , vol.122 , pp. 1565-1571
    • Ru, M.T.1    Hirokane, S.Y.2    Lo, A.S.3    Dordick, J.S.4    Reimer, J.A.5    Clark, D.S.6
  • 25
    • 0036001088 scopus 로고    scopus 로고
    • Plant responses to abiotic stresses: Heavy metal-induced oxidative stress and protection by mycorrhization
    • Schützendübel, A., & Polle, A. (2002). Plant responses to abiotic stresses: heavy metal-induced oxidative stress and protection by mycorrhization. Journal of Experimental Botany, 53, 1351-1365.
    • (2002) Journal of Experimental Botany , vol.53 , pp. 1351-1365
    • Schützendübel, A.1    Polle, A.2
  • 26
    • 0028206873 scopus 로고
    • The oligosaccharides of the Fe (III)-Zn(II) purple acid phosphatase of the red kidney bean - determination of the structure by a combination of matrix-assisted laser-desorption ionization mass-spectrometry and selective enzymatic degradation
    • Stahl, B., Klabunde, T., Witzel, H., Krebs, B., Steup, M., Karas, M., & Hillenkamp, F. (1994). The oligosaccharides of the Fe (III)-Zn(II) purple acid phosphatase of the red kidney bean - determination of the structure by a combination of matrix-assisted laser-desorption ionization mass-spectrometry and selective enzymatic degradation. European Journal of Biochemistry, 220, 321-330.
    • (1994) European Journal of Biochemistry , vol.220 , pp. 321-330
    • Stahl, B.1    Klabunde, T.2    Witzel, H.3    Krebs, B.4    Steup, M.5    Karas, M.6    Hillenkamp, F.7
  • 27
    • 0035150288 scopus 로고    scopus 로고
    • Influence of vegetation on low-molecular-weight carboxylic acids in soil solution: A review
    • Strobel, B.W. (2001). Influence of vegetation on low-molecular-weight carboxylic acids in soil solution: a review. Geoderma, 99, 169-198.
    • (2001) Geoderma , vol.99 , pp. 169-198
    • Strobel, B.W.1
  • 28
    • 0001081456 scopus 로고
    • Resolution and some properties of acid phosphatase isozymes bound to the cell wall of potato tubers
    • Sugawara, S., Inamoto, Y., & Ushijima, M. (1981). Resolution and some properties of acid phosphatase isozymes bound to the cell wall of potato tubers. Agricultural Biology Chemistry, 45, 1767-1774.
    • (1981) Agricultural Biology Chemistry , vol.45 , pp. 1767-1774
    • Sugawara, S.1    Inamoto, Y.2    Ushijima, M.3
  • 29
    • 0019888476 scopus 로고
    • Purification, enzymatic properties, and active site environment of a novel manganese (III)-containing acid phosphatase
    • Sugiura, Y., Kawabe, H., Tanaka, H., Fujimoto, S., & Ohara, A. (1981). Purification, enzymatic properties, and active site environment of a novel manganese (III)-containing acid phosphatase. Journal of Biology and Chemistry, 256, 10664-10670.
    • (1981) Journal of Biology and Chemistry , vol.256 , pp. 10664-10670
    • Sugiura, Y.1    Kawabe, H.2    Tanaka, H.3    Fujimoto, S.4    Ohara, A.5
  • 30
    • 0030813124 scopus 로고    scopus 로고
    • Isolation and characterization of a group III isozyme of acid phosphatase from rice plants
    • Tso, S., & Chen, Y. (1997). Isolation and characterization of a group III isozyme of acid phosphatase from rice plants. Botanical Bulletin of Academia Sinica, 38, 245-250.
    • (1997) Botanical Bulletin of Academia Sinica , vol.38 , pp. 245-250
    • Tso, S.1    Chen, Y.2
  • 31
    • 0016171450 scopus 로고
    • Studies on violet-coloured acid phosphatase of sweet potato. I. Purification and some physical properties
    • Uehara, K., Fujimoto, S., & Taniguchi, T. (1974). Studies on violet-coloured acid phosphatase of sweet potato. I. Purification and some physical properties. Journal of Biochemistry, 75, 627-638.
    • (1974) Journal of Biochemistry , vol.75 , pp. 627-638
    • Uehara, K.1    Fujimoto, S.2    Taniguchi, T.3
  • 32
    • 0038748235 scopus 로고    scopus 로고
    • Partial purification and kinetic characterization of acid phosphatase from garlic seedling
    • Yenigün, B., & Güvenilir, Y. (2003). Partial purification and kinetic characterization of acid phosphatase from garlic seedling. Applied Biochemistry and Biotechnology, 105-108, 677-687.
    • (2003) Applied Biochemistry and Biotechnology , vol.105-108 , pp. 677-687
    • Yenigün, B.1    Güvenilir, Y.2
  • 33
    • 0037853323 scopus 로고    scopus 로고
    • An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases
    • Zambonelli, C., & Roberts, M.F. (2003). An iron-dependent bacterial phospholipase D reminiscent of purple acid phosphatases. Journal of Biological Chemistry, 278, 13706-13711.
    • (2003) Journal of Biological Chemistry , vol.278 , pp. 13706-13711
    • Zambonelli, C.1    Roberts, M.F.2


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