메뉴 건너뛰기




Volumn 119, Issue 1-2, 1996, Pages 67-77

Purification and some properties of wheat germ acid phosphatases

Author keywords

Phosphatase isozymes; Wheat germ

Indexed keywords

ACID PHOSPHATASE; EPITOPE;

EID: 0030596835     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/0168-9452(96)04477-9     Document Type: Article
Times cited : (22)

References (29)
  • 1
    • 0019888476 scopus 로고
    • Purification, enzymatic properties, and active site environment of a new manganese(III)-containing acid phosphatase
    • [1] Y. Sugiura, H. Kawabe, H. Tanaka, S. Fujimoto and A. Ohara, Purification, enzymatic properties, and active site environment of a new manganese(III)-containing acid phosphatase. J. Biol. Chem., 256 (1981) 10664-10670.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10664-10670
    • Sugiura, Y.1    Kawabe, H.2    Tanaka, H.3    Fujimoto, S.4    Ohara, A.5
  • 2
    • 0011279597 scopus 로고
    • The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds
    • [2] D.H. Turner and J.F. Turner, The hydrolysis of glucose monophosphates by a phosphatase preparation from pea seeds. Biochem. J., 74 (1960) 486-491.
    • (1960) Biochem. J. , vol.74 , pp. 486-491
    • Turner, D.H.1    Turner, J.F.2
  • 3
    • 0002686771 scopus 로고
    • Exocellular enzymes of corn roots
    • [3] C.W. Chang and R.S. Bandurski, Exocellular enzymes of corn roots. Plant Physiol., 39 (1964) 60-64.
    • (1964) Plant Physiol. , vol.39 , pp. 60-64
    • Chang, C.W.1    Bandurski, R.S.2
  • 4
    • 0002567292 scopus 로고
    • Direct absorption of organic phosphate by rice and jute plants
    • [4] A. Islam, R. Mandal and K.T. Osman, Direct absorption of organic phosphate by rice and jute plants. Plant Soil, 53 (1979) 49-54.
    • (1979) Plant Soil , vol.53 , pp. 49-54
    • Islam, A.1    Mandal, R.2    Osman, K.T.3
  • 5
    • 0028005901 scopus 로고
    • Acid phosphatase activity in bean and cowpea plants grown under phosphorus stress
    • [5] D.S. Fernandez and J. Ascencio, Acid phosphatase activity in bean and cowpea plants grown under phosphorus stress. J. Plant Nutr., 17 (1994) 229-241.
    • (1994) J. Plant Nutr. , vol.17 , pp. 229-241
    • Fernandez, D.S.1    Ascencio, J.2
  • 6
    • 0000418323 scopus 로고
    • Purification and characterization of phosphatase in aleurone particles of rice grains
    • [6] H. Yamagata, K. Tanaka and Z. Kasai, Purification and characterization of phosphatase in aleurone particles of rice grains. Plant Cell Physiol., 21 (1980) 1449-1460.
    • (1980) Plant Cell Physiol. , vol.21 , pp. 1449-1460
    • Yamagata, H.1    Tanaka, K.2    Kasai, Z.3
  • 7
    • 0011316256 scopus 로고
    • Multiple forms of acid phosphatase in cotyledons of Vigna mungo seedlings
    • [7] T. Tamura, T. Minamikawa and T. Koshiba, Multiple forms of acid phosphatase in cotyledons of Vigna mungo seedlings. J. Exp. Bot., 33 (1982) 1332-1339.
    • (1982) J. Exp. Bot. , vol.33 , pp. 1332-1339
    • Tamura, T.1    Minamikawa, T.2    Koshiba, T.3
  • 8
    • 0011278902 scopus 로고
    • The wheat leaf phosphatases: VI the effect of metal ions on the acid phosphatase activity of dialyzed juice
    • [8] D.W.A. Roberts, The wheat leaf phosphatases: VI The effect of metal ions on the acid phosphatase activity of dialyzed juice. J. Biol. Chem., 230 (1958) 213-218.
    • (1958) J. Biol. Chem. , vol.230 , pp. 213-218
    • Roberts, D.W.A.1
  • 9
    • 0011286219 scopus 로고
    • Isolation and partial characterization of cytoplasmic and wall-bound acid phosphatases from wheat roots
    • [9] Y. Hasegawa, K.R. Lynn and W.J. Brockbank, Isolation and partial characterization of cytoplasmic and wall-bound acid phosphatases from wheat roots. Can. J. Bot., 54 (1976) 1163-1169.
    • (1976) Can. J. Bot. , vol.54 , pp. 1163-1169
    • Hasegawa, Y.1    Lynn, K.R.2    Brockbank, W.J.3
  • 10
    • 84971098582 scopus 로고
    • Leaf acid phosphatase isozymes in the diagnosis of phosphorus status in field-grown wheat
    • [10] K.D. Mclachlan, D.E., Elliott, D.G. De Marco and J.H. Garran, Leaf acid phosphatase isozymes in the diagnosis of phosphorus status in field-grown wheat. Aust. J. Agric. Res., 38 (1987) 1-13.
    • (1987) Aust. J. Agric. Res. , vol.38 , pp. 1-13
    • McLachlan, K.D.1    Elliott, D.E.2    De Marco, D.G.3    Garran, J.H.4
  • 11
    • 0011280118 scopus 로고
    • Purification and properties of a nonspecific acid phosphatase from wheat germ
    • [11] B.K. Joyce and S. Grisolla, Purification and properties of a nonspecific acid phosphatase from wheat germ. J. Biol. Chem., 235 (1960) 2278-2281.
    • (1960) J. Biol. Chem. , vol.235 , pp. 2278-2281
    • Joyce, B.K.1    Grisolla, S.2
  • 12
    • 0011361181 scopus 로고
    • Immunochemical differences in acid phosphatase isozymes from wheat germ
    • [12] T. Akiyama and S. Yamamoto, Immunochemical differences in acid phosphatase isozymes from wheat germ. Agric. Biol. Chem., 50 (1986) 437-440.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 437-440
    • Akiyama, T.1    Yamamoto, S.2
  • 13
    • 0025834737 scopus 로고
    • Isolation and characterization of a homogeneous isozyme of wheat germ acid phosphatase
    • [13] P.P. Waymack and R.L. Van Etten, Isolation and characterization of a homogeneous isozyme of wheat germ acid phosphatase. Arch. Biochem. Biophys., 288 (1991) 621-633.
    • (1991) Arch. Biochem. Biophys. , vol.288 , pp. 621-633
    • Waymack, P.P.1    Van Etten, R.L.2
  • 14
    • 0011285142 scopus 로고
    • Soluble proteins and multiple forms in early growth of wheat
    • [14] V. Macko, G.R. Honold and M.A. Stahmann, Soluble proteins and multiple forms in early growth of wheat. Phytochemistry, 6 (1967) 465-476.
    • (1967) Phytochemistry , vol.6 , pp. 465-476
    • Macko, V.1    Honold, G.R.2    Stahmann, M.A.3
  • 15
    • 0011373532 scopus 로고
    • Gibberellic acid-induced increase in activity of a particular isozyme of acid phosphatase in wheat half-seeds
    • [15] T. Akiyama, H. Uchimiya and H. Suzuki, Gibberellic acid-induced increase in activity of a particular isozyme of acid phosphatase in wheat half-seeds. Plant Cell Physiol., 22 (1981) 1023-1028.
    • (1981) Plant Cell Physiol. , vol.22 , pp. 1023-1028
    • Akiyama, T.1    Uchimiya, H.2    Suzuki, H.3
  • 16
    • 0028954219 scopus 로고
    • A long-lived batch reaction system of cell-free protein synthesis
    • [16] Y. Kawarasaki, T. Kawai, H. Nakano and T. Yamane, A long-lived batch reaction system of cell-free protein synthesis. Anal. Biochem., 226 (1995) 320-324.
    • (1995) Anal. Biochem. , vol.226 , pp. 320-324
    • Kawarasaki, Y.1    Kawai, T.2    Nakano, H.3    Yamane, T.4
  • 17
    • 85007941447 scopus 로고
    • Prolonged cell-free protein synthesis in a batch system using wheat germ extract
    • [17] Y. Kawarasaki, H. Nakano and T. Yamane, Prolonged cell-free protein synthesis in a batch system using wheat germ extract. Biosci. Biotech. Biochem., 58 (1994) 1911-1913.
    • (1994) Biosci. Biotech. Biochem. , vol.58 , pp. 1911-1913
    • Kawarasaki, Y.1    Nakano, H.2    Yamane, T.3
  • 18
    • 85007974354 scopus 로고
    • An increased rate of cell-free protein synthesis by condensing wheat-germ extract with ultrafiltration membranes
    • [18] H. Nakano, T. Tanaka, Y. Kawarasaki and T. Yamane, An increased rate of cell-free protein synthesis by condensing wheat-germ extract with ultrafiltration membranes. Biosci. Biotech. Biochem., 58 (1994) 631-634.
    • (1994) Biosci. Biotech. Biochem. , vol.58 , pp. 631-634
    • Nakano, H.1    Tanaka, T.2    Kawarasaki, Y.3    Yamane, T.4
  • 19
    • 0017128381 scopus 로고
    • Purification and properties of the proton - Translocating adenosine triphosphatase complex of bovine heart mitochondria
    • [19] R. Serrano, B.I. Kanner and E, Racker, Purification and properties of the proton - translocating adenosine triphosphatase complex of bovine heart mitochondria. J. Biol. Chem., 251 (1976) 2453-2461.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2453-2461
    • Serrano, R.1    Kanner, B.I.2    Racker, E.3
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • [20] M.M. Bradford, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing 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
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • [21] U.K. Laemmli, 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
  • 22
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • [22] W.N. Burnette, "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem., 112 (1981) 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 23
    • 0020671498 scopus 로고
    • Preparation of a cell-free protein-synthesizing system for wheat germ
    • [23] C.W. Anderson, J.W. Straus and B.S. Dudock, Preparation of a cell-free protein-synthesizing system for wheat germ. Methods Enzymol., 101 (1983) 635-644.
    • (1983) Methods Enzymol. , vol.101 , pp. 635-644
    • Anderson, C.W.1    Straus, J.W.2    Dudock, B.S.3
  • 24
    • 0017154853 scopus 로고
    • A sensitive fluorescent method for detection of glycoproteins in polyacrylamide gels
    • [24] A.E. Eckhardt, C.E. Hayes and I.J. Goldstein, A sensitive fluorescent method for detection of glycoproteins in polyacrylamide gels. Anal. Biochem., 73 (1976) 192-197.
    • (1976) Anal. Biochem. , vol.73 , pp. 192-197
    • Eckhardt, A.E.1    Hayes, C.E.2    Goldstein, I.J.3
  • 25
    • 0011280579 scopus 로고
    • Preparation and some properties of an acid phosphatase from white lupine seedlings
    • [25] M.Z. Newmark and B.S. Wenger, Preparation and some properties of an acid phosphatase from white lupine seedlings. Arch. Biochem. Biophys., 89 (1960) 110-117.
    • (1960) Arch. Biochem. Biophys. , vol.89 , pp. 110-117
    • Newmark, M.Z.1    Wenger, B.S.2
  • 26
    • 0013958662 scopus 로고
    • Acid phosphatase from tobacco leaves
    • [26] J.G. Shaw, Acid phosphatase from tobacco leaves. Arch. Biochem. Biophys., 117 (1966) 1-9.
    • (1966) Arch. Biochem. Biophys. , vol.117 , pp. 1-9
    • Shaw, J.G.1
  • 27
    • 0014662470 scopus 로고
    • Dio9 and chlorhexidine: Inhibitors of membrane-bound ATPase and cation transport in streptococcus faecalis
    • [27] F.M. Harold, J.R. Baarda, C. Baron and A. Abrams, Dio9 and chlorhexidine: inhibitors of membrane-bound ATPase and cation transport in Streptococcus faecalis. Biochim. Biophys. Acta, 183 (1969) 129-136.
    • (1969) Biochim. Biophys. Acta , vol.183 , pp. 129-136
    • Harold, F.M.1    Baarda, J.R.2    Baron, C.3    Abrams, A.4
  • 29
    • 0029942135 scopus 로고    scopus 로고
    • High productive cell-free synthesis system using condensed wheat-germ extract
    • in press
    • [29] H. Nakano, T. Tanaka, Y. Kawarasaki and T. Yamane, High productive cell-free synthesis system using condensed wheat-germ extract. J. Biotechnol., in press.
    • J. Biotechnol.
    • Nakano, H.1    Tanaka, T.2    Kawarasaki, Y.3    Yamane, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.