메뉴 건너뛰기




Volumn 15, Issue 3, 1998, Pages 357-365

A starch-accumulating mutant of Arabidopsis thaliana deficient in a chloroplastic starch-hydrolysing enzyme

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GLUCOSIDASE; AMYLASE; AMYLOPECTIN; BETA AMYLASE; CHLOROPLAST; ENZYME DEGRADATION; ENZYME SPECIFICITY; HYDROLYSIS; MUTANT; PHOSPHORYLASE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PULLULANASE; STARCH;

EID: 0032143523     PISSN: 09607412     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-313X.1998.00213.x     Document Type: Article
Times cited : (184)

References (34)
  • 2
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Bernfeld, P. (1955) Amylases, α and β. Methods Enzymol. 1, 149-158.
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 3
    • 0002135275 scopus 로고
    • Alterations in growth, photosynthesis and respiration in a starchless mutant of Arabidopsis thaliana (L) deficient in chloroplast phosphogluco-mutase activity
    • Caspar, T., Huber, S.C. and Somerville, C.R. (1985) Alterations in growth, photosynthesis and respiration in a starchless mutant of Arabidopsis thaliana (L) deficient in chloroplast phosphogluco- mutase activity. Plant Physiol. 79, 11-17.
    • (1985) Plant Physiol , vol.79 , pp. 11-17
    • Caspar, T.1    Huber, S.C.2    Somerville, C.R.3
  • 6
    • 0000668044 scopus 로고
    • Specific determination of a- Amylase activity in crude plant extracts containing β-amylase
    • Doehlert, D.C. and Duke, S.H. (1983) Specific determination of a- amylase activity in crude plant extracts containing β-amylase. Plant Physiol. 71, 229-234.
    • (1983) Plant Physiol , vol.71 , pp. 229-234
    • Doehlert, D.C.1    Duke, S.H.2
  • 7
    • 0029347013 scopus 로고
    • Biochemical and molecular characterisation of a novel starch synthase from potato tubers
    • Edwards, A., Marshall, J., Sidebottom, C., Visser, R.G.F., Smith, A.M. and Martin, C. (1995) Biochemical and molecular characterisation of a novel starch synthase from potato tubers. Plant J. 8, 283-294.
    • (1995) Plant J , vol.8 , pp. 283-294
    • Edwards, A.1    Marshall, J.2    Sidebottom, C.3    Visser, R.G.F.4    Smith, A.M.5    Martin, C.6
  • 8
    • 0029187334 scopus 로고
    • Monogenic recessive mutations causing both late floral initiation and excess starch accumulation in Arabidopsis
    • Eimert, K., Wang, S.-M., Lue, W.-L. and Chen, J. (1995) Monogenic recessive mutations causing both late floral initiation and excess starch accumulation in Arabidopsis. Plant Cell, 7, 1703-1712.
    • (1995) Plant Cell , vol.7 , pp. 1703-1712
    • Eimert, K.1    Wang, S.-M.2    Lue, W.-L.3    Chen, J.4
  • 9
    • 0348024041 scopus 로고
    • Determination of the A:B chain ratio of amylopectin and glycogen
    • BeMiller, J.N., Manners, D.J. and Sturgeon, R.J., eds. New York: Wiley
    • Enevoldsen, B.S. and Manners, D.J. (1994) Determination of the A:B chain ratio of amylopectin and glycogen. In Methods in Carbohydrate Chemistry, Volume X (BeMiller, J.N., Manners, D.J. and Sturgeon, R.J., eds). New York: Wiley, pp. 127-135.
    • (1994) Methods in Carbohydrate Chemistry , vol.10 , pp. 127-135
    • Enevoldsen, B.S.1    Manners, D.J.2
  • 10
    • 0001740843 scopus 로고
    • Turnover of starch and sucrose in the roots of Pisum saiivum
    • Hargreaves, J.A. and ap Rees, T. (1988) Turnover of starch and sucrose in the roots of Pisum saiivum. Phytochemistry, 27, 1627-1629.
    • (1988) Phytochemistry , vol.27 , pp. 1627-1629
    • Hargreaves, J.A.1    Ap Rees, T.2
  • 11
    • 0030483926 scopus 로고    scopus 로고
    • The onset of sucrose accumulation in cold-stored potato tubers is caused by an increased rate of sucrose synthesis and coincides with low levels of hexose-phosphates, an activation of sucrose phosphate synthase and the appearance of a new form of amylase
    • Hill, L.M., Reimholz, R., Schröder, R., Nielsen, T.H. and Stitt, M. (1996) The onset of sucrose accumulation in cold-stored potato tubers is caused by an increased rate of sucrose synthesis and coincides with low levels of hexose-phosphates, an activation of sucrose phosphate synthase and the appearance of a new form of amylase. Plant Cell Environ. 19, 1223-1237.
    • (1996) Plant Cell Environ. , vol.19 , pp. 1223-1237
    • Hill, L.M.1    Reimholz, R.2    Schröder, R.3    Nielsen, T.H.4    Stitt, M.5
  • 12
    • 0027951459 scopus 로고
    • Caution on the use of the generally accepted methanol precipitation technique for the assay of soluble starch synthase in crude extracts of plant tissues
    • Jenner, C.F., Denyer, K. and Hawker, J.S. (1994) Caution on the use of the generally accepted methanol precipitation technique for the assay of soluble starch synthase in crude extracts of plant tissues. Aust. J. Plant Physiol. 21, 17-22.
    • (1994) Aust. J. Plant Physiol. , vol.21 , pp. 17-22
    • Jenner, C.F.1    Denyer, K.2    Hawker, J.S.3
  • 13
    • 0001328805 scopus 로고
    • Electrophoretic transfer as a technique for the detection and identification of plant amylolytic enzymes in polyacrylamide gels
    • Kakefuda, G. and Duke, S.H. (1984) Electrophoretic transfer as a technique for the detection and identification of plant amylolytic enzymes in polyacrylamide gels. Plant Physiol. 75, 278-280.
    • (1984) Plant Physiol , vol.75 , pp. 278-280
    • Kakefuda, G.1    Duke, S.H.2
  • 14
    • 0000955301 scopus 로고    scopus 로고
    • Partial purification and characterisation of a diurnally fluctuating novel endoamylase from Arabidopsis thaliana leaves
    • Kakefuda, G. and Preiss, J. (1997) Partial purification and characterisation of a diurnally fluctuating novel endoamylase from Arabidopsis thaliana leaves. Plant Physiol. Biochem. 35, 907-913.
    • (1997) Plant Physiol. Biochem. , vol.35 , pp. 907-913
    • Kakefuda, G.1    Preiss, J.2
  • 15
    • 0041111584 scopus 로고
    • Properties of α-glucan phosphorylase from pea chloroplasts
    • Kruger, N.J. and ap Rees, T. (1983a) Properties of α-glucan phosphorylase from pea chloroplasts. Phytochemistry, 22, 1891-1898.
    • (1983) Phytochemistry , vol.22 , pp. 1891-1898
    • Kruger, N.J.1    Ap Rees, T.2
  • 16
    • 0001725393 scopus 로고
    • Maltose metabolism by pea chloroplasts
    • Kruger, N.J. and ap Rees, T. (1983b) Maltose metabolism by pea chloroplasts. Planta, 158, 179-184.
    • (1983) Planta , vol.158 , pp. 179-184
    • Kruger, N.J.1    Ap Rees, T.2
  • 17
    • 0008531390 scopus 로고
    • Amylopectin degradation in pea chloroplast extracts
    • Levi, C. and Preiss, J. (1978) Amylopectin degradation in pea chloroplast extracts. Plant Physiol. 61, 218-220.
    • (1978) Plant Physiol. , vol.61 , pp. 218-220
    • Levi, C.1    Preiss, J.2
  • 18
    • 0001489664 scopus 로고
    • Characterisation and subcellular localisation of debranching enzyme and endoamylase from the leaves of sugar beet
    • Li, B., Servaites, J.C. and Geiger, D.R. (1992) Characterisation and subcellular localisation of debranching enzyme and endoamylase from the leaves of sugar beet. Plant Physiol. 98, 1277-1284.
    • (1992) Plant Physiol. , vol.98 , pp. 1277-1284
    • Li, B.1    Servaites, J.C.2    Geiger, D.R.3
  • 19
    • 0007671216 scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase in greening Zea mays leaves
    • Lin, C.H. and Stocking, C.R. (1980) Glyceraldehyde-3-phosphate dehydrogenase in greening Zea mays leaves. Plant Physiol. 65, 897-901.
    • (1980) Plant Physiol. , vol.65 , pp. 897-901
    • Lin, C.H.1    Stocking, C.R.2
  • 20
    • 0001117527 scopus 로고
    • Isolation and characterisation of a starchless mutant of Arabidopsis thaliana (L.) Heynh. lacking ADPglucose pyrophosphorylase activity
    • Lin, T.-P., Caspar, T., Somerville, C. and Preiss, J. (1988a) Isolation and characterisation of a starchless mutant of Arabidopsis thaliana (L.) Heynh. lacking ADPglucose pyrophosphorylase activity. Plant Physiol. 86, 1131-1135.
    • (1988) Plant Physiol , vol.86 , pp. 1131-1135
    • Lin, T.-P.1    Caspar, T.2    Somerville, C.3    Preiss, J.4
  • 21
    • 0000231796 scopus 로고
    • Subcellular localisation and characterisation of amylases in Arabidopsis leaf
    • Lin, T.-P., Spilatro, S.R. and Preiss, J. (1988c) Subcellular localisation and characterisation of amylases in Arabidopsis leaf. Plant Physiol. 86, 251-259.
    • (1988) Plant Physiol , vol.86 , pp. 251-259
    • Lin, T.-P.1    Spilatro, S.R.2    Preiss, J.3
  • 22
    • 0009466084 scopus 로고
    • Purification of β-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism
    • Monroe, J.D. and Preiss, J. (1990) Purification of β-amylase that accumulates in Arabidopsis thaliana mutants defective in starch metabolism. Plant Physiol. 94, 1099-1039.
    • (1990) Plant Physiol , vol.94 , pp. 1099-11039
    • Monroe, J.D.1    Preiss, J.2
  • 23
    • 0001004433 scopus 로고
    • Subcellular localisation of the starch degradative and biosynthetic enzymes of spinach leaves
    • Okita, T.W., Greenberg, E., Kuhn, D.N. and Preiss, J. (1979) Subcellular localisation of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiol. 64, 187-192.
    • (1979) Plant Physiol , vol.64 , pp. 187-192
    • Okita, T.W.1    Greenberg, E.2    Kuhn, D.N.3    Preiss, J.4
  • 24
    • 0001481929 scopus 로고
    • Major differences in isoforms of starch- Branching enzymes in embryos of round- and wrinkled-seeded peas (Pisum sativum L.)
    • Smith, A.M. (1988) Major differences in isoforms of starch- branching enzymes in embryos of round- and wrinkled-seeded peas (Pisum sativum L.). Planta, 175, 270-279.
    • (1988) Planta , vol.175 , pp. 270-279
    • Smith, A.M.1
  • 25
    • 0003203125 scopus 로고
    • Starch degrading enzymes
    • Steup, M. (1990) Starch degrading enzymes. Methods Plant Biochem. 3, 103-128.
    • (1990) Methods Plant Biochem , vol.3 , pp. 103-128
    • Steup, M.1
  • 26
    • 0020839257 scopus 로고
    • Multiple forms of amylase in leaf extracts: Electrophoretic transfer of the enzyme forms into amylose-containing polyacrylamide gels
    • Steup, M. and Gerbling, K.-P. (1983) Multiple forms of amylase in leaf extracts: electrophoretic transfer of the enzyme forms into amylose-containing polyacrylamide gels. Anal. Biochem. 134, 96-100.
    • (1983) Anal. Biochem. , vol.134 , pp. 96-100
    • Steup, M.1    Gerbling, K.-P.2
  • 27
    • 0019327356 scopus 로고
    • Carbohydrate breakdown by chloroplasts of Pisum sativum
    • Stitt, M. and ap Rees, T. (1978) Carbohydrate breakdown by chloroplasts of Pisum sativum. Biochim. Blophys. Acta, 627, 131-143.
    • (1978) Biochim. Blophys. Acta , vol.627 , pp. 131-143
    • Stitt, M.1    Ap Rees, T.2
  • 28
    • 0001250491 scopus 로고
    • Physiological rates of starch breakdown in isolated intact spinach chloroplasts
    • Stitt, M. and Heldt, H.W. (1981) Physiological rates of starch breakdown in isolated intact spinach chloroplasts. Plant Physiol. 68, 755-761.
    • (1981) Plant Physiol , vol.68 , pp. 755-761
    • Stitt, M.1    Heldt, H.W.2
  • 29
    • 0028843003 scopus 로고
    • The role of the chloroplasta-glucosidase in transitory starch degradation
    • Sun, Z., Duke, S.H. and Henson, C.A. (1995) The role of the chloroplasta-glucosidase in transitory starch degradation. Plant Physiol. 108, 211-217.
    • (1995) Plant Physiol , vol.108 , pp. 211-217
    • Sun, Z.1    Duke, S.H.2    Henson, C.A.3
  • 30
    • 0027458378 scopus 로고
    • Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato
    • Takaha, T., Yanase, M., Okada, S. and Smith, S.M. (1993) Disproportionating enzyme (4-α-glucanotransferase; EC 2.4.1.25) of potato. J. Biol. Chem. 268, 1391-1396.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1391-1396
    • Takaha, T.1    Yanase, M.2    Okada, S.3    Smith, S.M.4
  • 31
    • 0027978717 scopus 로고
    • A mutant of Arabidopsis lacking the ability to transport glucose across the chloroplast envelope
    • Trethewey, R.N. and ap Rees, T. (1994a) A mutant of Arabidopsis lacking the ability to transport glucose across the chloroplast envelope. Biochem. J. 301, 449-454.
    • (1994) Biochem. J. , vol.301 , pp. 449-454
    • Trethewey, R.N.1    Ap Rees, T.2
  • 32
    • 0028191115 scopus 로고
    • The role of the hexose transporter in the chloroplasts of Arabidopsis thaliana
    • Trethewey, R.N. and ap Rees, T. (1994b) The role of the hexose transporter in the chloroplasts of Arabidopsis thaliana. Planta, 195, 168-174.
    • (1994) Planta , vol.195 , pp. 168-174
    • Trethewey, R.N.1    Ap Rees, T.2
  • 33
    • 0001069489 scopus 로고
    • Isolation of intact chloroplasts - General principles and criteria of integrity
    • Walker, D.A., Cerovic, Z.G. and Robinson, S.P. (1987) Isolation of intact chloroplasts - general principles and criteria of integrity. Methods Enzymol. 148, 145-157.
    • (1987) Methods Enzymol , vol.148 , pp. 145-157
    • Walker, D.A.1    Cerovic, Z.G.2    Robinson, S.P.3
  • 34
    • 0000662190 scopus 로고
    • Organ specificity of starch branching enzyme (Q-enzyme) in rice
    • Yamanouchi, H. and Nakamura, Y. (1992) Organ specificity of starch branching enzyme (Q-enzyme) in rice. Plant Cell Physiol. 33, 985-991.
    • (1992) Plant Cell Physiol , vol.33 , pp. 985-991
    • Yamanouchi, H.1    Nakamura, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.