메뉴 건너뛰기




Volumn 1, Issue 2, 2002, Pages 188-196

Role of disulfide bridges in structure-activity relationship of plant lipases from wheat germ and rice bran

Author keywords

Activity; Conformational stability; Disulfide bond; Lipase; Rice bran; Thermal stability; Wheat germ

Indexed keywords

DISULFIDE; TRIACYLGLYCEROL LIPASE;

EID: 0042316732     PISSN: 09725849     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (3)

References (34)
  • 1
    • 0009202382 scopus 로고
    • Biochemical studies on rice bran lipase Part II. Chemical properties
    • Aizono Y et al, 1971. Biochemical studies on rice bran lipase Part II. Chemical properties. Agric Biol Chem, 35, 1973-1979.
    • (1971) Agric Biol Chem , vol.35 , pp. 1973-1979
    • Aizono, Y.1
  • 2
    • 0015817011 scopus 로고
    • Enzymatic properties of rice bran lipase
    • Aizono Y et al, 1973. Enzymatic properties of rice bran lipase. Agric Biol Chem, 37, 2031-2036.
    • (1973) Agric Biol Chem , vol.37 , pp. 2031-2036
    • Aizono, Y.1
  • 3
    • 0017188808 scopus 로고
    • Purification and charterization of rice bran lipase part II
    • Aizono Y et al, 1976. Purification and charterization of rice bran lipase part II. Agric Biol Chem, 40, 317-324.
    • (1976) Agric Biol Chem , vol.40 , pp. 317-324
    • Aizono, Y.1
  • 4
    • 0031032679 scopus 로고    scopus 로고
    • A two-stage mechanism for the reductive unfolding of disulfide containing proteins
    • Chang J-Y, 1997. A two-stage mechanism for the reductive unfolding of disulfide containing proteins. J Biol Chem, 272, 69-75.
    • (1997) J Biol Chem , vol.272 , pp. 69-75
    • Chang, J.-Y.1
  • 5
    • 0015230487 scopus 로고
    • A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism
    • Chen Y H & Yang J T, 1971. A new approach to the calculation of secondary structures of globular proteins by optical rotatory dispersion and circular dichroism. Biochem Biophys Res Commun, 44, 1285-1291.
    • (1971) Biochem Biophys Res Commun , vol.44 , pp. 1285-1291
    • Chen, Y.H.1    Yang, J.T.2
  • 6
    • 0014013802 scopus 로고
    • Tryptophan residues in native and Reoxidized Muramidase: Luminescence properties
    • Churchich J E, 1966. Tryptophan residues in native and Reoxidized Muramidase: Luminescence properties. Biochim Biophys Acta, 120, 406-412.
    • (1966) Biochim Biophys Acta , vol.120 , pp. 406-412
    • Churchich, J.E.1
  • 7
    • 0014008783 scopus 로고
    • Fluorescence and protein structure IX. Relationship between tyrosine fluorescence and various stages in denaturation of Ribonuclease
    • Cowgill R W, 1966. Fluorescence and protein structure IX. Relationship between tyrosine fluorescence and various stages in denaturation of Ribonuclease. Biochim Biophys Acta, 120, 196-211.
    • (1966) Biochim Biophys Acta , vol.120 , pp. 196-211
    • Cowgill, R.W.1
  • 8
    • 0017819733 scopus 로고
    • Chemical properties of major subunits of rice bran lipase
    • Fujiki Y et al, 1978. Chemical properties of major subunits of rice bran lipase. Agric Biol Chem, 42, 599-606.
    • (1978) Agric Biol Chem , vol.42 , pp. 599-606
    • Fujiki, Y.1
  • 9
    • 0001201872 scopus 로고
    • Biochemical studies on rice bran lipase. Part I. Purification and physical properties
    • Funatsu M et al, 1971. Biochemical studies on rice bran lipase. Part I. Purification and physical properties. Agric Biol Chem, 35, 734-742.
    • (1971) Agric Biol Chem , vol.35 , pp. 734-742
    • Funatsu, M.1
  • 10
    • 0006224362 scopus 로고
    • Avidin quenching of fluorescence by dinitrophenyl groups
    • Green N M, 1964. Avidin quenching of fluorescence by dinitrophenyl groups. Biochem J, 90, 564-568.
    • (1964) Biochem J , vol.90 , pp. 564-568
    • Green, N.M.1
  • 11
    • 0014030213 scopus 로고
    • Chemical evaluation of conformational differences in native and chemically modified proteins
    • Habeeb A F S A, 1966. Chemical evaluation of conformational differences in native and chemically modified proteins. Biochim Biophys Acta, 115, 440-454.
    • (1966) Biochim Biophys Acta , vol.115 , pp. 440-454
    • Habeeb, A.F.S.A.1
  • 13
    • 0025019350 scopus 로고
    • Conformational stability of globular proteins
    • Pace C N, 1990. Conformational stability of globular proteins. Trends Biochem Sci, 15, 14-17.
    • (1990) Trends Biochem Sci , vol.15 , pp. 14-17
    • Pace, C.N.1
  • 15
    • 0023783477 scopus 로고
    • Conformational stability and activity of ribonuclease
    • Pace C N et al, 1988. Conformational stability and activity of ribonuclease. J Biol Chem, 263,11820-11825.
    • (1988) J Biol Chem , vol.263 , pp. 11820-11825
    • Pace, C.N.1
  • 16
    • 0032493315 scopus 로고    scopus 로고
    • Roles of individual disulfide bonds in the stability and folding of ω-conotoxin Goldenberg D P
    • Price-Carter M & Hull M S, 1998. Roles of individual disulfide bonds in the stability and folding of ω-conotoxin Goldenberg D P. Biochemistry, 37, 9851-9861.
    • (1998) Biochemistry , vol.37 , pp. 9851-9861
    • Price-Carter, M.1    Hull, M.S.2
  • 17
    • 0025689397 scopus 로고
    • Effect of pH in the acidic region on the structural integrity of lipase from wheat germ
    • Rajendran S et al, 1990. Effect of pH in the acidic region on the structural integrity of lipase from wheat germ. Indian J Biochem Biophys, 27, 300-310.
    • (1990) Indian J Biochem Biophys , vol.27 , pp. 300-310
    • Rajendran, S.1
  • 18
    • 0042271270 scopus 로고
    • Ph D Thesis, University of Mysore, Mysore, India
    • Rajeshwara A N, 1994. Ph D Thesis, University of Mysore, Mysore, India.
    • (1994)
    • Rajeshwara, A.N.1
  • 19
  • 20
    • 84984500027 scopus 로고
    • Purification and characterization of lipase from rice (Oryza sativa L.) bran
    • Rajeshwara A N & Prakash V, 1995. Purification and characterization of lipase from rice (Oryza sativa L.) bran. Die Nahrung, 39, 406-418.
    • (1995) Die Nahrung , vol.39 , pp. 406-418
    • Rajeshwara, A.N.1    Prakash, V.2
  • 21
    • 0000895720 scopus 로고    scopus 로고
    • Effect of denaturant and cosolvent on the stability of wheat germ lipase
    • Rajeshwara A N & Prakash V, 1996. Effect of denaturant and cosolvent on the stability of wheat germ lipase. J Agric Food Chem, 44, 736-740.
    • (1996) J Agric Food Chem , vol.44 , pp. 736-740
    • Rajeshwara, A.N.1    Prakash, V.2
  • 22
    • 0030004366 scopus 로고    scopus 로고
    • Preferential interaction of denaturants with rice bran lipase
    • Rajeshwara A N et al, 1996. Preferential interaction of denaturants with rice bran lipase. Int J Biol Macromol, 19, 1-7.
    • (1996) Int J Biol Macromol , vol.19 , pp. 1-7
    • Rajeshwara, A.N.1
  • 23
    • 0019889475 scopus 로고
    • Kinetic correlations between the disulfide bond reduction and the induced conformational change of proteins
    • Segawa T et al, 1992. Kinetic correlations between the disulfide bond reduction and the induced conformational change of proteins. Biochim Biophys Acta, 668, 89-97.
    • (1992) Biochim Biophys Acta , vol.668 , pp. 89-97
    • Segawa, T.1
  • 25
    • 0001591890 scopus 로고
    • Chemical Studies of rice bran lipase
    • Shastry B S & Rao M R R, 1976. Chemical Studies of rice bran lipase. Cereal Chem, 53, 190-200.
    • (1976) Cereal Chem , vol.53 , pp. 190-200
    • Shastry, B.S.1    Rao, M.R.R.2
  • 26
    • 0006055093 scopus 로고    scopus 로고
    • Selenol-catalyzed reduction of disulfide bonds in peptides and proteins
    • edited by D R Marshak. Academic Press Inc, California, USA
    • Singh R, 1996. Selenol-catalyzed Reduction of Disulfide Bonds in Peptides and Proteins. in Techniques in Protein Chemistry VII, edited by D R Marshak. Academic Press Inc, California, USA. Pp 221-230.
    • (1996) Techniques in Protein Chemistry VII , pp. 221-230
    • Singh, R.1
  • 27
    • 0023644891 scopus 로고
    • Conformations of intermediates in the folding of the pancreatic trypsin inhibitor
    • States D J et al, 1987. Conformations of intermediates in the folding of the pancreatic trypsin inhibitor. J Mol Biol, 195, 731-739.
    • (1987) J Mol Biol , vol.195 , pp. 731-739
    • States, D.J.1
  • 28
    • 0002944544 scopus 로고
    • Structural transitions of lysozyme
    • Steiner R F, 1964. Structural transitions of lysozyme. Biochim Biophys Acta, 79, 51-63.
    • (1964) Biochim Biophys Acta , vol.79 , pp. 51-63
    • Steiner, R.F.1
  • 29
    • 0025821855 scopus 로고
    • Structural stability of lipase from wheat germ in alkaline pH
    • Sudhindra Rao K et al, 1991. Structural stability of lipase from wheat germ in alkaline pH. J Protein Chem, 10, 291-299.
    • (1991) J Protein Chem , vol.10 , pp. 291-299
    • Rao, K.S.1
  • 30
    • 0025897562 scopus 로고
    • Role of an intrachain disulfide bond in the conformation and stability of ovalbumin
    • Takahashi N et al, 1991. Role of an intrachain disulfide bond in the conformation and stability of ovalbumin. J Biochem, 109, 846-851.
    • (1991) J Biochem , vol.109 , pp. 846-851
    • Takahashi, N.1
  • 31
    • 0019881763 scopus 로고
    • Disulfide bridges in globular proteins
    • Thornton J M, 1981. Disulfide bridges in globular proteins. J Mol Biol, 151, 261-287.
    • (1981) J Mol Biol , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 32
    • 0013889663 scopus 로고
    • A specific method for serum lipase determination
    • Tietz N W & Fiereck E A, 1966. A specific method for serum lipase determination. Clin Chim Acta, 13, 352-358.
    • (1966) Clin Chim Acta , vol.13 , pp. 352-358
    • Tietz, N.W.1    Fiereck, E.A.2
  • 33
    • 0001227472 scopus 로고
    • Harnessing disulfide bonds using protein engineering
    • Wetzel R, 1987. Harnessing disulfide bonds using protein engineering. Trends Biochem Sci, 12, 478-482.
    • (1987) Trends Biochem Sci , vol.12 , pp. 478-482
    • Wetzel, R.1
  • 34
    • 0028972081 scopus 로고
    • Phospholipase A2 engineering. The roles of disulfide bonds in structure, conformational stability and catalytic function
    • Zhu H et al, 1995. Phospholipase A2 engineering. The roles of disulfide bonds in structure, conformational stability and catalytic function. Biochemistry, 34, 15307-15314.
    • (1995) Biochemistry , vol.34 , pp. 15307-15314
    • Zhu, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.