메뉴 건너뛰기




Volumn 1388, Issue 2, 1998, Pages 457-464

Subunit composition and oligomer stability of oat β-glucosidase isozymes

Author keywords

Glucosidase; Heteromultimer; Homomultimer; Isozyme; Oat

Indexed keywords

ALANINE; BETA GLUCOSIDASE; CALCIUM CHLORIDE; ISOENZYME; LYSINE; OLIGOMER; UREA;

EID: 0032506206     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00209-X     Document Type: Article
Times cited : (13)

References (24)
  • 1
    • 0002731955 scopus 로고
    • The fine structure of chloroplast stroma following aldehyde osmium-tetroxide fixation
    • Gunning B.E.S. The fine structure of chloroplast stroma following aldehyde osmium-tetroxide fixation. J. Cell Biol. 24:1965;79-93.
    • (1965) J. Cell Biol. , vol.24 , pp. 79-93
    • Gunning, B.E.S.1
  • 2
    • 0000230852 scopus 로고
    • Immunocytological and chemical studies on the stromacentre-forming protein from Avena plastid
    • Nisius A., Ruppel H.G. Immunocytological and chemical studies on the stromacentre-forming protein from Avena plastid. Planta. 171:1987;443-452.
    • (1987) Planta , vol.171 , pp. 443-452
    • Nisius, A.1    Ruppel, H.G.2
  • 3
    • 0000449964 scopus 로고
    • The stromacentre in Avena plastids: An aggregation of β-glucosidase responsible for the activation of oat-leaf saponins
    • Nisius A. The stromacentre in Avena plastids: an aggregation of β-glucosidase responsible for the activation of oat-leaf saponins. Planta. 173:1988;474-481.
    • (1988) Planta , vol.173 , pp. 474-481
    • Nisius, A.1
  • 4
    • 0000634721 scopus 로고    scopus 로고
    • Purification and characterization of isoenzyme of β-glucosidase from etiolated oat seedlings
    • Kim Y.-W., Song P.-S., Kim I.-S. Purification and characterization of isoenzyme of β-glucosidase from etiolated oat seedlings. Mol. Cells. 6:1996;773-779.
    • (1996) Mol. Cells , vol.6 , pp. 773-779
    • Kim, Y.-W.1    Song, P.-S.2    Kim, I.-S.3
  • 5
    • 0000994164 scopus 로고
    • Characterization of a protein-kinase activity associated with phytochrome from etiolated oat (Avena sativa L.) seedlings
    • Grimm R., Gast D., Rüdiger W. Characterization of a protein-kinase activity associated with phytochrome from etiolated oat (Avena sativa L.) seedlings. Planta. 178:1989;199-206.
    • (1989) Planta , vol.178 , pp. 199-206
    • Grimm, R.1    Gast, D.2    Rüdiger, W.3
  • 6
    • 0027919427 scopus 로고
    • A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form
    • Mummert E., Grimm E., Speth V., Eckerskorn C., Schiltz E., Gatenby A.A., Schafer E. A TCP1-related molecular chaperone from plants refolds phytochrome to its photoreversible form. Nature. 363:1993;644-648.
    • (1993) Nature , vol.363 , pp. 644-648
    • Mummert, E.1    Grimm, E.2    Speth, V.3    Eckerskorn, C.4    Schiltz, E.5    Gatenby, A.A.6    Schafer, E.7
  • 7
    • 0028307973 scopus 로고
    • The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone copurified with phytochrome belongs to a β-glucosidase
    • Gus-Mayer S., Brunner H., Schneider-Poetsch H.A.W., Lottspeich F., Eckerskorn C., Grimm R., Rüdiger W. The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone copurified with phytochrome belongs to a β-glucosidase. FEBS Lett. 374:1994;51-54.
    • (1994) FEBS Lett. , vol.374 , pp. 51-54
    • Gus-Mayer, S.1    Brunner, H.2    Schneider-Poetsch, H.A.W.3    Lottspeich, F.4    Eckerskorn, C.5    Grimm, R.6    Rüdiger, W.7
  • 8
    • 0028535437 scopus 로고
    • Avenacosidase from oat: Purification, sequence analysis and biochemical characterization of a new member of the BGA family of β-glucosidase
    • Gus-Mayer S., Brunner H., Schneider-Poetsch H.A.W., Rüdiger W. Avenacosidase from oat: purification, sequence analysis and biochemical characterization of a new member of the BGA family of β-glucosidase. Plant Mol. Biol. 26:1994;909-921.
    • (1994) Plant Mol. Biol. , vol.26 , pp. 909-921
    • Gus-Mayer, S.1    Brunner, H.2    Schneider-Poetsch, H.A.W.3    Rüdiger, W.4
  • 10
    • 0000823370 scopus 로고
    • Prunus serotina amigdalin hydrolase and prunasin hydrolase
    • Li C.P., Swain E., Poulton J.E. Prunus serotina amigdalin hydrolase and prunasin hydrolase. Plant Physiol. 100:1992;282-290.
    • (1992) Plant Physiol. , vol.100 , pp. 282-290
    • Li, C.P.1    Swain, E.2    Poulton, J.E.3
  • 11
    • 0027547488 scopus 로고
    • Characterization of a Brassica napus myrosinase pseudogene: Myrosinases are member of the BGA family of β-glycosidase
    • Lenman M., Falk A., Rask L. Characterization of a Brassica napus myrosinase pseudogene: myrosinases are member of the BGA family of β-glycosidase. Plant Mol. Biol. 21:1993;463-574.
    • (1993) Plant Mol. Biol. , vol.21 , pp. 463-574
    • Lenman, M.1    Falk, A.2    Rask, L.3
  • 12
    • 0000878877 scopus 로고
    • A protein from maize labeled with azido-IAA has novel β-glucosidase activity
    • Campos N., Bako L., Feldwisch J., Schell J., Palme K. A protein from maize labeled with azido-IAA has novel β-glucosidase activity. Plant J. 2:1992;675-694.
    • (1992) Plant J. , vol.2 , pp. 675-694
    • Campos, N.1    Bako, L.2    Feldwisch, J.3    Schell, J.4    Palme, K.5
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0000925011 scopus 로고
    • Analysis of protein conformation by gel electrophoresis
    • in: T.E. Creighton (Ed.), IRL press, Oxford
    • D.O. Goldenberg, Analysis of protein conformation by gel electrophoresis, in: T.E. Creighton (Ed.), Protein Structure, IRL press, Oxford, 1989, pp. 225-250.
    • (1989) Protein Structure , pp. 225-250
    • Goldenberg, D.O.1
  • 17
    • 0029240490 scopus 로고
    • A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin
    • Dharmawardhana D.P., Ellis B.E., Carlson J.E. A β-glucosidase from lodgepole pine xylem specific for the lignin precursor coniferin. Plant Physiol. 107:1995;313-339.
    • (1995) Plant Physiol. , vol.107 , pp. 313-339
    • Dharmawardhana, D.P.1    Ellis, B.E.2    Carlson, J.E.3
  • 19
    • 77957002357 scopus 로고
    • Carboxypeptidase A and B
    • Ambler R.P. Carboxypeptidase A and B. Methods Enzymol. 25:1972;262-272.
    • (1972) Methods Enzymol. , vol.25 , pp. 262-272
    • Ambler, R.P.1
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0025080896 scopus 로고
    • Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): Amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II
    • Ferri G., Stoppini M., Meloni M., Zapponi M.C., Iadarola P. Chloroplast glyceraldehyde-3-phosphate dehydrogenase (NADP): amino acid sequence of the subunits from isoenzyme I and structural relationship with isoenzyme II. Biochim. Biophys. Acta. 1041:1990;36-42.
    • (1990) Biochim. Biophys. Acta , vol.1041 , pp. 36-42
    • Ferri, G.1    Stoppini, M.2    Meloni, M.3    Zapponi, M.C.4    Iadarola, P.5
  • 22
    • 0000788621 scopus 로고
    • Light activation and molecular-mass changes of NAD(P)-glyceraldehyde-3-phosphate dehydrogenase of spinach and maize leaves
    • Scagliarini S., Trost P., Pupillo P., Valenti V. Light activation and molecular-mass changes of NAD(P)-glyceraldehyde-3-phosphate dehydrogenase of spinach and maize leaves. Planta. 190:1993;313-319.
    • (1993) Planta , vol.190 , pp. 313-319
    • Scagliarini, S.1    Trost, P.2    Pupillo, P.3    Valenti, V.4
  • 24
    • 0031277449 scopus 로고    scopus 로고
    • Expression and characterization of pea chloroplast glyceraldehyde-3-phosphate dehydrogenase composed of only the B-subunit
    • Li A.D., Anderson L.E. Expression and characterization of pea chloroplast glyceraldehyde-3-phosphate dehydrogenase composed of only the B-subunit. Plant Physiol. 115:1997;1201-1209.
    • (1997) Plant Physiol. , vol.115 , pp. 1201-1209
    • Li, A.D.1    Anderson, L.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.