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Volumn 9, Issue 2, 2000, Pages 93-98

One step purification of peanut phospholipase D by precipitation with alginate

Author keywords

Protein precipitation by polymer; Reversibly soluble insoluble polymer; Titrimetric assay

Indexed keywords

ALGINIC ACID; CABBAGE; CALCIUM; CARROT; ENZYME ACTIVITY; ENZYME BINDING; ENZYME PURIFICATION; PEANUT; PHOSPHATIDYLCHOLINE; PHOSPHOLIPASE D; POLYMER; PRECIPITATION; SODIUM CHLORIDE; SOYBEAN; WHEAT GERM;

EID: 0034041286     PISSN: 0923179X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1008121005974     Document Type: Article
Times cited : (21)

References (30)
  • 1
    • 0018802932 scopus 로고
    • Phospholipase D from Savoy cabbage: Purification and preliminary kinetic characterization
    • Allyger, T.T. and Wells, M. A. (1979) Phospholipase D from Savoy cabbage: Purification and preliminary kinetic characterization. Biochemistry 18: 5348-5353.
    • (1979) Biochemistry , vol.18 , pp. 5348-5353
    • Allyger, T.T.1    Wells, M.A.2
  • 2
    • 0033559641 scopus 로고    scopus 로고
    • The determination of phospholipase D activity in emulsion systems
    • Aurich I, Hirche F and Ulbrich-Hofmann R (1999) The determination of phospholipase D activity in emulsion systems. Anal. Biochem. 268: 337-342.
    • (1999) Anal. Biochem. , vol.268 , pp. 337-342
    • Aurich, I.1    Hirche, F.2    Ulbrich-Hofmann, R.3
  • 3
    • 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
  • 5
    • 0031945051 scopus 로고    scopus 로고
    • Kinetic analysis in mixed micelles of partially purified rat brain phospholipase D activity and its activation by phosphatidylinositol 4,5-bisphosphate
    • Chalifa-Caspi V, Eli Y and Liscovitch M (1998) Kinetic analysis in mixed micelles of partially purified rat brain phospholipase D activity and its activation by phosphatidylinositol 4,5-bisphosphate. Neurochem. Res. 23: 589-599.
    • (1998) Neurochem. Res. , vol.23 , pp. 589-599
    • Chalifa-Caspi, V.1    Eli, Y.2    Liscovitch, M.3
  • 6
    • 0003751067 scopus 로고
    • Worthington Biochemical Corp., Free hold, New Jersey
    • Decker LA (1977) Worthington Enzyme Manual. Worthington Biochemical Corp., pp 173-176, Free hold, New Jersey.
    • (1977) Worthington Enzyme Manual , pp. 173-176
    • Decker, L.A.1
  • 7
    • 0033553482 scopus 로고    scopus 로고
    • G-protein-stimulated phospholipase D activity is inhibited by lethal toxin from Clostridium sordellii in HL-60 cells
    • El Hadj NB, Popoff MR, Marvaud JC, Payrastre B, Boquet P and Geny B (1999) G-protein-stimulated phospholipase D activity is inhibited by lethal toxin from Clostridium sordellii in HL-60 cells. J. Biol. Chem. 274: 14021-14031.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14021-14031
    • El Hadj, N.B.1    Popoff, M.R.2    Marvaud, J.C.3    Payrastre, B.4    Boquet, P.5    Geny, B.6
  • 8
    • 0030948743 scopus 로고    scopus 로고
    • New developments in phospholipase D
    • Exton JH (1997a) New developments in phospholipase D. J. Biol. Chem. 272: 15579-15582.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15579-15582
    • Exton, J.H.1
  • 9
    • 0030892164 scopus 로고    scopus 로고
    • Phospholipase D: Enzymology, mechanisms of regulation, and function
    • Exton JH (1997b) Phospholipase D: enzymology, mechanisms of regulation, and function. Physiol. Rev. 77: 303-320.
    • (1997) Physiol. Rev. , vol.77 , pp. 303-320
    • Exton, J.H.1
  • 10
    • 0344654709 scopus 로고    scopus 로고
    • The platelet-activating factor receptor antagonist L-659, 989 inhibits phospholipase D activity
    • Gomez-Munoz A, O'Brien L and Steinbrecher UP (1999) The platelet-activating factor receptor antagonist L-659, 989 inhibits phospholipase D activity. Biochim. Biophys. Acta. 1438: 247-252.
    • (1999) Biochim. Biophys. Acta , vol.1438 , pp. 247-252
    • Gomez-Munoz, A.1    O'Brien, L.2    Steinbrecher, U.P.3
  • 11
    • 0027729562 scopus 로고
    • Purification of endo-polygalacturonase by affinity precipitation using alginate. Biotechnol
    • Gupta MN, Guoqiang D and Mattiasson B (1993) Purification of endo-polygalacturonase by affinity precipitation using alginate. Biotechnol. Appl. Biochem. 18: 321-327.
    • (1993) Appl. Biochem. , vol.18 , pp. 321-327
    • Gupta, M.N.1    Guoqiang, D.2    Mattiasson, B.3
  • 14
    • 0019200937 scopus 로고
    • A convenient spectrophotometric assay for phospholipase D using p-nitrophenylphosphorylcholine as substrate
    • Gupta MN and Wold F (1980) A convenient spectrophotometric assay for phospholipase D using p-nitrophenylphosphorylcholine as substrate. Lipids 15: 594-596.
    • (1980) Lipids , vol.15 , pp. 594-596
    • Gupta, M.N.1    Wold, F.2
  • 15
    • 0344438749 scopus 로고
    • The action of lecithinase D on lecithin. The enzymatic preparation of D-1,2-Dipalmitolein and D-1,2-Dipalmitin
    • Hanahan DJ and Vercamer R (1954) The action of lecithinase D on lecithin. The enzymatic preparation of D-1,2-Dipalmitolein and D-1,2-Dipalmitin. J. Amer. Chem.Soc. 76: 1804-1806.
    • (1954) J. Amer. Chem.Soc. , vol.76 , pp. 1804-1806
    • Hanahan, D.J.1    Vercamer, R.2
  • 16
    • 0346818016 scopus 로고
    • Phospholipase D from peanut seeds
    • Heller M, Mozes N and Maes E (1969) Phospholipase D from peanut seeds. Methods Enzymol. 14: 226-234.
    • (1969) Methods Enzymol. , vol.14 , pp. 226-234
    • Heller, M.1    Mozes, N.2    Maes, E.3
  • 17
    • 0001619404 scopus 로고
    • Phospholipase D from peanut seeds: IV Final purification and some properties of the enzyme
    • Heller M, Mozes N, Peri I and Maes E (1974) Phospholipase D from peanut seeds: IV Final purification and some properties of the enzyme. Biochim. Biophys. Acta. 369: 397-410.
    • (1974) Biochim. Biophys. Acta , vol.369 , pp. 397-410
    • Heller, M.1    Mozes, N.2    Peri, I.3    Maes, E.4
  • 18
    • 0025886699 scopus 로고
    • Solubilisation and purification of rat tissue phospholipase D
    • Dennis EA (ed)
    • Kobayashi M and Kanfer JN (1991) Solubilisation and purification of rat tissue phospholipase D. In: Dennis EA (ed) Methods in Enzymol. 197: 575-583.
    • (1991) Methods in Enzymol. , vol.197 , pp. 575-583
    • Kobayashi, M.1    Kanfer, J.N.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0030954947 scopus 로고    scopus 로고
    • Identification and characterization of a novel plant phospholipase D that requires polyphosphoinositides and submicromolar calcium for activity in Arabidopsis
    • Pappan K, Zheng S and Wang X (1997) Identification and characterization of a novel plant phospholipase D that requires polyphosphoinositides and submicromolar calcium for activity in Arabidopsis. J. Biol. Chem. 272: 7048-7054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7048-7054
    • Pappan, K.1    Zheng, S.2    Wang, X.3
  • 22
    • 0025953368 scopus 로고
    • Affinity precipitation of extracellular microbial enzymes
    • Pecs M, Eggert M and Schugerl K (1991) Affinity precipitation of extracellular microbial enzymes. J. Biotechnol. 21: 137-142.
    • (1991) J. Biotechnol. , vol.21 , pp. 137-142
    • Pecs, M.1    Eggert, M.2    Schugerl, K.3
  • 25
    • 0032446815 scopus 로고    scopus 로고
    • Alginate beads as an affinity material for alpha amylases
    • Sardar M and Gupta MN (1998) Alginate beads as an affinity material for alpha amylases. Bioseparation 7: 159-165.
    • (1998) Bioseparation , vol.7 , pp. 159-165
    • Sardar, M.1    Gupta, M.N.2
  • 27
    • 0025391442 scopus 로고
    • Alginate as immoblization matrix for cells
    • Smidsrod O and Skjak-Braek G (1990) Alginate as immoblization matrix for cells. Trends. Biotechnol. 8: 71-78.
    • (1990) Trends. Biotechnol. , vol.8 , pp. 71-78
    • Smidsrod, O.1    Skjak-Braek, G.2
  • 28
    • 0025037298 scopus 로고
    • Interesterification of phosphatidylcholine with lipases in organic media
    • Svensson I, Aldercreutz P and Mattiasson B (1990) Interesterification of phosphatidylcholine with lipases in organic media. Appl. Microbiol. Biotechnol. 33: 255-258.
    • (1990) Appl. Microbiol. Biotechnol. , vol.33 , pp. 255-258
    • Svensson, I.1    Aldercreutz, P.2    Mattiasson, B.3
  • 29
    • 0025768760 scopus 로고
    • A continuous spectrophotometric method for monitoring phospholipase D-catalysed reactions of physiological substrates
    • Takrama JF and Taylor KE (1991) A continuous spectrophotometric method for monitoring phospholipase D-catalysed reactions of physiological substrates. J. Biophys. Methods. 23: 217-226.
    • (1991) J. Biophys. Methods. , vol.23 , pp. 217-226
    • Takrama, J.F.1    Taylor, K.E.2
  • 30
    • 0023656686 scopus 로고
    • Purification of phospholipase D from citrus callus tissue
    • Witt W, Yelenosky G and Mayer RT (1987) Purification of phospholipase D from citrus callus tissue. Arch. Biochem. Biophys. 259: 164-170.
    • (1987) Arch. Biochem. Biophys. , vol.259 , pp. 164-170
    • Witt, W.1    Yelenosky, G.2    Mayer, R.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.