메뉴 건너뛰기




Volumn 44, Issue 11, 1996, Pages 3489-3493

Kinetic and Structural Studies on Thermal Inactivation of Lipoxygenase L1: Effect of Nonionic Surfactants

Author keywords

Lipoxygenase; Nonionic surfactants; Thermal inactivation

Indexed keywords

GLYCINE MAX;

EID: 2542626626     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf950450o     Document Type: Article
Times cited : (4)

References (27)
  • 2
    • 0015621272 scopus 로고
    • Heat inactivation of trypsin inhibitor,lipoxygenase and urease in soybeans: Effect of acid and base additives
    • Baker, E. C.; Mustakas, G. C. Heat inactivation of trypsin inhibitor,lipoxygenase and urease in soybeans: effect of acid and base additives. J. Am, Oil Chem. Soc. 1973, 50, 137-141.
    • (1973) J. Am, Oil Chem. Soc. , vol.50 , pp. 137-141
    • Baker, E.C.1    Mustakas, G.C.2
  • 3
    • 0027246677 scopus 로고
    • The three dimensional structure of an arachidonic acid 15 lipoxygenase
    • Boyington, J. C.; Gaffney, B. J.; Amzel, L. M. The three dimensional structure of an arachidonic acid 15 lipoxygenase. Science 1993, 260, 1482-1486.
    • (1993) Science , vol.260 , pp. 1482-1486
    • Boyington, J.C.1    Gaffney, B.J.2    Amzel, L.M.3
  • 4
    • 51249186592 scopus 로고
    • Minimizing protein insolubilization during thermal inactivation of lipoxygenase in soybean cotyledons
    • Brown, B. D.; Wei, L. S.; Steinberg, M. P.; Villota, R. Minimizing protein insolubilization during thermal inactivation of lipoxygenase in soybean cotyledons. J. Am. Oil Chem. Soc. 1982, 59, 88-92.
    • (1982) J. Am. Oil Chem. Soc. , vol.59 , pp. 88-92
    • Brown, B.D.1    Wei, L.S.2    Steinberg, M.P.3    Villota, R.4
  • 5
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, R. J. Proteins as molecular chaperones. Nature 1987, 328, 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, R.J.1
  • 7
  • 8
    • 0040180173 scopus 로고
    • Inactivation of lipoxygenase and trypsin inhibitor in soybeans on microwave irradiation
    • Esaka, M.; Suziki, K.; Kubota, K. Inactivation of lipoxygenase and trypsin inhibitor in soybeans on microwave irradiation. Agric. Biol. Chem. 1986, 50, 2395-2396.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 2395-2396
    • Esaka, M.1    Suziki, K.2    Kubota, K.3
  • 9
    • 0025741241 scopus 로고
    • Recent investigations into the lipoxygenase pathway of plants
    • Gardner, H. W. Recent investigations into the lipoxygenase pathway of plants. Biochim. Biophys. Acta 1991, 1084, 221-239.
    • (1991) Biochim. Biophys. Acta , vol.1084 , pp. 221-239
    • Gardner, H.W.1
  • 10
    • 0023506457 scopus 로고
    • Folding and association of protiens
    • Jaenicke, R. Folding and association of protiens. Prog. Biophys. Mol. Biol. 1987, 49, 117-237.
    • (1987) Prog. Biophys. Mol. Biol. , vol.49 , pp. 117-237
    • Jaenicke, R.1
  • 11
    • 0002893631 scopus 로고
    • Folding proteins
    • Creighten, T. E., Ed.; IRL Press: Oxford
    • Jaenicke, R.; Rudolph, R. Folding proteins. In Protein Structure; Creighten, T. E., Ed.; IRL Press: Oxford, 1989; pp 191-223.
    • (1989) Protein Structure , pp. 191-223
    • Jaenicke, R.1    Rudolph, R.2
  • 13
    • 0017916757 scopus 로고
    • Solute quenching of protein fluorescence
    • Lehrer, S. S.; Leavis, P. C. Solute quenching of protein fluorescence. Methods Enzymol. 1978, 49, 222-236.
    • (1978) Methods Enzymol. , vol.49 , pp. 222-236
    • Lehrer, S.S.1    Leavis, P.C.2
  • 14
    • 0000124213 scopus 로고
    • Inactivation of peroxidase, lipoxygenase and polyphenol oxidase by manothermosonication
    • Lopez, P.; Sala, F. J.; de la Fuente, J. L.; Condon, S.; Raso, J.; Burgos, J. Inactivation of peroxidase, lipoxygenase and polyphenol oxidase by manothermosonication. J. Agric. Food Chem. 1994, 42, 252-256.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 252-256
    • Lopez, P.1    Sala, F.J.2    De La Fuente, J.L.3    Condon, S.4    Raso, J.5    Burgos, J.6
  • 15
    • 0003466969 scopus 로고
    • Prentice-Hall International: London
    • Moore, W. J. Physical Chemistry; Prentice-Hall International: London, 1962, pp 253-322.
    • (1962) Physical Chemistry , pp. 253-322
    • Moore, W.J.1
  • 16
    • 0026801413 scopus 로고
    • Limited proteolysis and active site labelling studies of soybean lipoxygenase 1
    • Ramachandran, S.; Carrol, R. T.; Dunham, W. R.; Funk, M. O. Limited proteolysis and active site labelling studies of soybean lipoxygenase 1. Biochemistry 1992, 31, 7700-7706.
    • (1992) Biochemistry , vol.31 , pp. 7700-7706
    • Ramachandran, S.1    Carrol, R.T.2    Dunham, W.R.3    Funk, M.O.4
  • 17
    • 0023177955 scopus 로고
    • Leucotrienes and lipoxins; structures biosynthesis and biological effects
    • Samuelsson, B.; Dahlen, S. E.; Lindgren, J. A.; Rouzer, C. A.; Serhan, C. N. Leucotrienes and lipoxins; structures biosynthesis and biological effects. Science 1987, 237, 1171-1176.
    • (1987) Science , vol.237 , pp. 1171-1176
    • Samuelsson, B.1    Dahlen, S.E.2    Lindgren, J.A.3    Rouzer, C.A.4    Serhan, C.N.5
  • 19
    • 0022503366 scopus 로고
    • Enzymology of reticulocyte lipoxygenase: Comparision with other lipoxygenase
    • Schewe, T.; Rapoport, S. M.; Kuhn, H. Enzymology of reticulocyte lipoxygenase: comparision with other lipoxygenase. Adv. Enzymol. 1986, 58, 191-272.
    • (1986) Adv. Enzymol. , vol.58 , pp. 191-272
    • Schewe, T.1    Rapoport, S.M.2    Kuhn, H.3
  • 20
    • 0028150110 scopus 로고
    • Effect of nonionic detergents on lipoxygenase catalysis
    • Schilstra, M. J.; Veldink, G. A.; Vliegenthart, J. F. G. Effect of nonionic detergents on lipoxygenase catalysis. Lipids 1994, 29, 225-231.
    • (1994) Lipids , vol.29 , pp. 225-231
    • Schilstra, M.J.1    Veldink, G.A.2    Vliegenthart, J.F.G.3
  • 22
    • 0001354276 scopus 로고
    • Kinetic and structural studies on the interaction of surfactants with lipoxygenase L1 from soybeans (Glycine max)
    • Srinivasulu, S.; Rao, A. G. A. Kinetic and structural studies on the interaction of surfactants with lipoxygenase L1 from soybeans (Glycine max). J. Agric. Food Chem, 1993, 41, 366-371.
    • (1993) J. Agric. Food Chem , vol.41 , pp. 366-371
    • Srinivasulu, S.1    Rao, A.G.A.2
  • 23
    • 0038565896 scopus 로고    scopus 로고
    • The detection of kinetic intermediates during the unfolding of lipoxygenase-1 by urea or quanidine hydrochloride
    • Srinivasulu, S.; Rao, A. G. A. The detection of kinetic intermediates during the unfolding of lipoxygenase-1 by urea or quanidine hydrochloride. Biochim. Biophys. Acta 1996, 1294, 115-120.
    • (1996) Biochim. Biophys. Acta , vol.1294 , pp. 115-120
    • Srinivasulu, S.1    Rao, A.G.A.2
  • 24
    • 0015997959 scopus 로고
    • Aromatic contribution to circular dichroism spectra of proteins
    • Strickland, E. H. Aromatic contribution to circular dichroism spectra of proteins. Crit. Rev. Biochem. 1974, 2, 113-175.
    • (1974) Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 25
    • 0023030976 scopus 로고
    • Detergent assisted refolding of guanidinium chloride denatured rhodanese. The effect of laural maltoside
    • Tandon, S.; Horowitz, P. M. Detergent assisted refolding of guanidinium chloride denatured rhodanese. The effect of laural maltoside. J. Biol. Chem. 1986, 261, 15615-15618.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15615-15618
    • Tandon, S.1    Horowitz, P.M.2
  • 26
    • 0023255917 scopus 로고
    • Detergent assisted refolding of guanidinium chloride denatured rhodanese. The effect of concentration and detergent
    • Tandon, S.; Horowitz, P. M. Detergent assisted refolding of guanidinium chloride denatured rhodanese. The effect of concentration and detergent. J. Biol. Chem. 1987, 262, 4486-4491.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4486-4491
    • Tandon, S.1    Horowitz, P.M.2
  • 27
    • 0002669974 scopus 로고
    • Lipoxygenases
    • Pryor, W. A., Ed.; Academic Press: New York
    • Vliegenthart, J. F. G.; Veldink, G. A. Lipoxygenases. In Free Radicals in Biology; Pryor, W. A., Ed.; Academic Press: New York, 1982; Vol. 5, pp 29-64.
    • (1982) Free Radicals in Biology , vol.5 , pp. 29-64
    • Vliegenthart, J.F.G.1    Veldink, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.