메뉴 건너뛰기




Volumn 214, Issue 2, 2001, Pages 243-249

Purification and characterization of banana fruit acid phosphatase

Author keywords

Acid phosphatase; Banana (ripening); Carbohydrate metabolism; Musa (fruit); Phosphate metabolism

Indexed keywords

ABSORPTION; ENZYMES; FRUITS; GELS; MONOMERS; PH EFFECTS; PHOSPHATES; PROTEINS; PURIFICATION;

EID: 0035786885     PISSN: 00320935     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004250100607     Document Type: Article
Times cited : (40)

References (37)
  • 2
    • 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
  • 4
    • 0027092553 scopus 로고
    • A simple computer program with statistical tests for the analysis of enzyme kinetics
    • Brooks SPG (1992) A simple computer program with statistical tests for the analysis of enzyme kinetics. Biotechniques 13:906-911
    • (1992) Biotechniques , vol.13 , pp. 906-911
    • Brooks, S.P.G.1
  • 5
    • 0026531719 scopus 로고
    • Bound and determined: A computer program for making buffers of defined ion concentration
    • Brooks SPG, Storey KB (1992) Bound and determined: A computer program for making buffers of defined ion concentration. Anal Biochem 201:119-126
    • (1992) Anal Biochem , vol.201 , pp. 119-126
    • Brooks, S.P.G.1    Storey, K.B.2
  • 6
    • 0000428663 scopus 로고
    • Senescence. Association of synthesis of acid phosphatase with banana ripening
    • De Leo P, Sacher JA (1970) Senescence. Association of synthesis of acid phosphatase with banana ripening. Plant Physiol 46:208-211
    • (1970) Plant Physiol , vol.46 , pp. 208-211
    • De Leo, P.1    Sacher, J.A.2
  • 7
    • 0033198547 scopus 로고    scopus 로고
    • A type 5 acid phosphatase gene from Arabidopsis thaliana is induced by phosphate starvation and by some other types of phosphate mobilising/oxidative stress conditions
    • del Pozo JC, Allona I, Rubio V, Leyva A, de la Pena A, Aragoncillo C, Paz-Ares J (1999) A type 5 acid phosphatase gene from Arabidopsis thaliana is induced by phosphate starvation and by some other types of phosphate mobilising/oxidative stress conditions. Plant J 19:579-589
    • (1999) Plant J , vol.19 , pp. 579-589
    • Del Pozo, J.C.1    Allona, I.2    Rubio, V.3    Leyva, A.4    De la Pena, A.5    Aragoncillo, C.6    Paz-Ares, J.7
  • 8
    • 0029115587 scopus 로고
    • Photometric microtiter assay of inorganic phosphate in the presence of acid-labile organic phosphates
    • Drueckes P, Schinzel R, Palm D (1995) Photometric microtiter assay of inorganic phosphate in the presence of acid-labile organic phosphates. Anal Biochem 230:173-177
    • (1995) Anal Biochem , vol.230 , pp. 173-177
    • Drueckes, P.1    Schinzel, R.2    Palm, D.3
  • 9
    • 0000618327 scopus 로고
    • Purification and characterisation of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells
    • Duff SMG, Lefebvre DD, Plaxton WC (1989) Purification and characterisation of a phosphoenolpyruvate phosphatase from Brassica nigra suspension cells. Plant Physiol 90:734-741
    • (1989) Plant Physiol , vol.90 , pp. 734-741
    • Duff, S.M.G.1    Lefebvre, D.D.2    Plaxton, W.C.3
  • 10
    • 0027950058 scopus 로고
    • The role of acid phosphatases in plant phosphorus metabolism
    • Duff SMG, Sarath G, Plaxton WC (1994) The role of acid phosphatases in plant phosphorus metabolism. Physiol Plant 90:791-800
    • (1994) Physiol Plant , vol.90 , pp. 791-800
    • Duff, S.M.G.1    Sarath, G.2    Plaxton, W.C.3
  • 11
    • 0033543704 scopus 로고    scopus 로고
    • Glycolytic intermediates as substrates of soybean acid phosphatase isoforms
    • Ferreira CV, Taga EM, Aoyama H (1999) Glycolytic intermediates as substrates of soybean acid phosphatase isoforms. Plant Sci 147:49-54
    • (1999) Plant Sci , vol.147 , pp. 49-54
    • Ferreira, C.V.1    Taga, E.M.2    Aoyama, H.3
  • 12
    • 0028140651 scopus 로고
    • Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity
    • Gellatly KS, Moorhead GBG, Duff SMG, Lefebvre DD, Plaxton WC (1994) Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity. Plant Physiol 106:223-232
    • (1994) Plant Physiol , vol.106 , pp. 223-232
    • Gellatly, K.S.1    Moorhead, G.B.G.2    Duff, S.M.G.3    Lefebvre, D.D.4    Plaxton, W.C.5
  • 13
    • 0023957340 scopus 로고
    • Purification and characterization of phytase from cotyledons of germinating soybean seeds
    • Gibson DM, Ullah AH (1988) Purification and characterization of phytase from cotyledons of germinating soybean seeds. Arch Biochem Biophys 260:503-513
    • (1988) Arch Biochem Biophys , vol.260 , pp. 503-513
    • Gibson, D.M.1    Ullah, A.H.2
  • 14
    • 0033405301 scopus 로고    scopus 로고
    • Purification and kinetic properties of a castor bean seed acid phosphatase containing sulfhydryl groups
    • Granjeiro PA, Ferreira CV, Granjeiro JM, Taga EM, Aoyama H (1999) Purification and kinetic properties of a castor bean seed acid phosphatase containing sulfhydryl groups. Physiol Plant 107:151-158
    • (1999) Physiol Plant , vol.107 , pp. 151-158
    • Granjeiro, P.A.1    Ferreira, C.V.2    Granjeiro, J.M.3    Taga, E.M.4    Aoyama, H.5
  • 15
    • 0031437530 scopus 로고    scopus 로고
    • Purification and characterization of an acid phosphatase from the bulb of Allium cepa L. var. Sweet Spanish
    • Guo J, Pesacreta TC (1997) Purification and characterization of an acid phosphatase from the bulb of Allium cepa L. var. Sweet Spanish. J Plant Physiol 151:520-527
    • (1997) J Plant Physiol , vol.151 , pp. 520-527
    • Guo, J.1    Pesacreta, T.C.2
  • 16
    • 0029136398 scopus 로고
    • Partial purification and characterization of an enzyme from pea nuclei with protein tyrosine phosphatase activity
    • Guo YL, Roux SJ (1995) Partial purification and characterization of an enzyme from pea nuclei with protein tyrosine phosphatase activity. Plant Physiol 107:167-175
    • (1995) Plant Physiol , vol.107 , pp. 167-175
    • Guo, Y.L.1    Roux, S.J.2
  • 17
    • 0030596835 scopus 로고    scopus 로고
    • Purification and some properties of wheat germ acid phosphatase
    • Kawarasaki Y, Nakano H, Yamane T (1996) Purification and some properties of wheat germ acid phosphatase. Plant Sci 119:67-77
    • (1996) Plant Sci , vol.119 , pp. 67-77
    • Kawarasaki, Y.1    Nakano, H.2    Yamane, T.3
  • 18
    • 0000360682 scopus 로고    scopus 로고
    • The dimetal center of purple acid phosphatases
    • Klabunde T, Krebs B (1997) The dimetal center of purple acid phosphatases. Struct Bonding. Berlin 89:177-198
    • (1997) Struct Bonding. Berlin , vol.89 , pp. 177-198
    • Klabunde, T.1    Krebs, B.2
  • 19
    • 0029003660 scopus 로고
    • Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases
    • Klabunde T, Strater N, Krebs B, Witzel H (1995) Structural relationship between the mammalian Fe(III)-Fe(II) and the Fe(III)-Zn(II) plant purple acid phosphatases. FEBS Lett 367:56-60
    • (1995) FEBS Lett , vol.367 , pp. 56-60
    • Klabunde, T.1    Strater, N.2    Krebs, B.3    Witzel, H.4
  • 20
    • 0029029080 scopus 로고
    • Purification and characterization of a novel phosphoenolpyruvate carboxylase from banana fruit
    • Law RD, Plaxton WC (1995) Purification and characterization of a novel phosphoenolpyruvate carboxylase from banana fruit. Biochem J 307:807-816
    • (1995) Biochem J , vol.307 , pp. 807-816
    • Law, R.D.1    Plaxton, W.C.2
  • 21
    • 0030752239 scopus 로고    scopus 로고
    • Regulatory phosphorylation of banana fruit phosphoenolpyruvate carboxylase by a copurifying phosphoenolpyruvate carboxylase-kinase
    • Law RD, Plaxton WC (1997) Regulatory phosphorylation of banana fruit phosphoenolpyruvate carboxylase by a copurifying phosphoenolpyruvate carboxylase-kinase. Eur J Biochem 247:642-651
    • (1997) Eur J Biochem , vol.247 , pp. 642-651
    • Law, R.D.1    Plaxton, W.C.2
  • 22
    • 0028262202 scopus 로고
    • Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism
    • Lindqvist Y, Schneider G, Vihko P (1994) Crystal structures of rat acid phosphatase complexed with the transition-state analogs vanadate and molybdate. Implications for the reaction mechanism. Eur J Biochem 221:139-142
    • (1994) Eur J Biochem , vol.221 , pp. 139-142
    • Lindqvist, Y.1    Schneider, G.2    Vihko, P.3
  • 23
    • 0023656258 scopus 로고
    • Effect of ethylene treatment on the concentration of fructose-2,6-bisphosphate and on the activity of phosphofructokinase-2/fructose-2,6-bisphosphatase in banana
    • Mertens E, Marcellin P, Van Schaftingen E, Hers HG (1987) Effect of ethylene treatment on the concentration of fructose-2,6-bisphosphate and on the activity of phosphofructokinase-2/fructose-2,6-bisphosphatase in banana. Eur J Biochem 167:579-583
    • (1987) Eur J Biochem , vol.167 , pp. 579-583
    • Mertens, E.1    Marcellin, P.2    Van Schaftingen, E.3    Hers, H.G.4
  • 27
    • 0001259453 scopus 로고    scopus 로고
    • The organization and regulation of plant glycolysis
    • Plaxton WC (1996) The organization and regulation of plant glycolysis. Annu Rev Plant Physiol Plant Mol Biol 47:185-214
    • (1996) Annu Rev Plant Physiol Plant Mol Biol , vol.47 , pp. 185-214
    • Plaxton, W.C.1
  • 29
    • 0015218654 scopus 로고
    • 3-Phosphoglycerate phosphatase in plants. I. Isolation and characterization from sugar cane leaves
    • Randall DD, Tolbert NE (1971) 3-Phosphoglycerate phosphatase in plants. I. Isolation and characterization from sugar cane leaves. J Biol Chem 246:5510-5517
    • (1971) J Biol Chem , vol.246 , pp. 5510-5517
    • Randall, D.D.1    Tolbert, N.E.2
  • 30
    • 0032768689 scopus 로고    scopus 로고
    • A histidine thiol 100 kDa, tetrameric acid phosphatase from lentil, Lens esculenta, seeds with the characteristics of protein tyrosine phosphatases
    • Roknabadi SM, Bose SK, Taneia V (1999) A histidine thiol 100 kDa, tetrameric acid phosphatase from lentil, Lens esculenta, seeds with the characteristics of protein tyrosine phosphatases. Biochim Biophys Acta 1433:272-280
    • (1999) Biochim Biophys Acta , vol.1433 , pp. 272-280
    • Roknabadi, S.M.1    Bose, S.K.2    Taneia, V.3
  • 32
    • 0031750396 scopus 로고    scopus 로고
    • Methyl jasmonate induces acid phosphatase activity in rice leaves
    • Shih C-Y, Kao HK (1997) Methyl jasmonate induces acid phosphatase activity in rice leaves. J Plant Physiol 152:358-362
    • (1997) J Plant Physiol , vol.152 , pp. 358-362
    • Shih, C.-Y.1    Kao, H.K.2
  • 33
    • 0027966810 scopus 로고
    • Purification of the major soybean leaf acid phosphatase that is increased by seedpod removal
    • Staswick PE, Papa C, Huang J-F, Rhee Y (1994) Purification of the major soybean leaf acid phosphatase that is increased by seedpod removal. Plant Physiol 104:49-57
    • (1994) Plant Physiol , vol.104 , pp. 49-57
    • Staswick, P.E.1    Papa, C.2    Huang, J.-F.3    Rhee, Y.4
  • 34
    • 0034672137 scopus 로고    scopus 로고
    • Purification and characterization of cytosolic pyruvate kinase from banana fruit
    • Turner WL, Plaxton WC (2000) Purification and characterization of cytosolic pyruvate kinase from banana fruit. Biochem J 352:875-882
    • (2000) Biochem J , vol.352 , pp. 875-882
    • Turner, W.L.1    Plaxton, W.C.2
  • 35
    • 0000519998 scopus 로고
    • Some properties of 3-phosphoglycerate phosphatase from developing rice grain
    • Villareal RM, Juliano BO (1977) Some properties of 3-phosphoglycerate phosphatase from developing rice grain. Plant Physiol 59:134-138
    • (1977) Plant Physiol , vol.59 , pp. 134-138
    • Villareal, R.M.1    Juliano, B.O.2
  • 36
    • 0025222988 scopus 로고
    • An enzyme with a double identity: Purple acid phosphatase and tartrate-resistant acid phosphatase
    • Vincent JB, Averill BA (1990) An enzyme with a double identity: Purple acid phosphatase and tartrate-resistant acid phosphatase. FASEB J 4:3009-3014
    • (1990) FASEB J , vol.4 , pp. 3009-3014
    • Vincent, J.B.1    Averill, B.A.2
  • 37
    • 0026535321 scopus 로고
    • Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions
    • Vincent JB, Crowder MW, Averill BA (1992) Hydrolysis of phosphate monoesters: A biological problem with multiple chemical solutions. Trends Biochem Sci 17:105-110
    • (1992) Trends Biochem Sci , vol.17 , pp. 105-110
    • Vincent, J.B.1    Crowder, M.W.2    Averill, B.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.