메뉴 건너뛰기




Volumn 5, Issue 7, 1996, Pages 1394-1405

Membrane-bound states of α-lactalbumin: Implications for the protein stability and conformation

Author keywords

fluorescence; lactose synthase; membranes; molten globule; lactalbumin

Indexed keywords

ACRYLAMIDE; ALPHA LACTALBUMIN; CALCIUM; CALCIUM CHLORIDE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; EGTAZIC ACID; LIPOSOME; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; TRYPTOPHAN; ZINC;

EID: 0030014802     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050718     Document Type: Article
Times cited : (53)

References (86)
  • 4
    • 0027536094 scopus 로고
    • Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study
    • Alexandrescu AT, Evans PA, Pitkeathly M, Baum J, Dobson CM. 1993. Structure and dynamics of the acid-denatured molten globule state of α-lactalbumin: A two-dimensional NMR study. Biochemistry 32:1707-1718.
    • (1993) Biochemistry , vol.32 , pp. 1707-1718
    • Alexandrescu, A.T.1    Evans, P.A.2    Pitkeathly, M.3    Baum, J.4    Dobson, C.M.5
  • 5
    • 0021510968 scopus 로고
    • Effect of orientational order on the decay of the fluorescence anisotropy in membrane suspensions. Experimental verification on unilamellar vesicles and lipid/α-lactalbumin complexes
    • Ameloot M, Hendrickx H, Herreman W, Pottel H, Van Cauwelaert F, Van der Meer WF. 1984. Effect of orientational order on the decay of the fluorescence anisotropy in membrane suspensions. Experimental verification on unilamellar vesicles and lipid/α-lactalbumin complexes. Biophys J 46:525-539.
    • (1984) Biophys J , vol.46 , pp. 525-539
    • Ameloot, M.1    Hendrickx, H.2    Herreman, W.3    Pottel, H.4    Van Cauwelaert, F.5    Van Der Meer, W.F.6
  • 6
    • 0029872515 scopus 로고    scopus 로고
    • NMR and stopped-flow studies of metal ion binding to α-lactabumins
    • Aramini JM, Hiraoki T, Vogel HJ. 1996. NMR and stopped-flow studies of metal ion binding to α-lactabumins. Biochem Biophys Acta 1293:72-82.
    • (1996) Biochem Biophys Acta , vol.1293 , pp. 72-82
    • Aramini, J.M.1    Hiraoki, T.2    Vogel, H.J.3
  • 7
    • 0015528068 scopus 로고
    • The modification of the tryptophan residues of bovine α-lactalbumin with 2-hydroxy-5-nitrobenzylbromide and with dimethyl(2-hydroxy-5-nitrobenzyl) sulphonium bromide. I. Characterization of the modified protein
    • Barman TE. 1972, The modification of the tryptophan residues of bovine α-lactalbumin with 2-hydroxy-5-nitrobenzylbromide and with dimethyl(2-hydroxy-5-nitrobenzyl) sulphonium bromide. I. Characterization of the modified protein. Biochim Biophys Acta 258:297-313.
    • (1972) Biochim Biophys Acta , vol.258 , pp. 297-313
    • Barman, T.E.1
  • 8
    • 0015531112 scopus 로고
    • The modification of the tryptophan residues of bovine α-lactalbumin with 2-hydroxy-5-nitrobenzylbromide and with dimethyl(2-hydroxy-5-nitrobenzyl)sulphonium bromide. II. Effect on the specifier protein activity
    • Barman TE, Bagshaw W. 1972. The modification of the tryptophan residues of bovine α-lactalbumin with 2-hydroxy-5-nitrobenzylbromide and with dimethyl(2-hydroxy-5-nitrobenzyl)sulphonium bromide. II. Effect on the specifier protein activity. Biochim Biophys Acta 278:491-500.
    • (1972) Biochim Biophys Acta , vol.278 , pp. 491-500
    • Barman, T.E.1    Bagshaw, W.2
  • 9
    • 0024533979 scopus 로고
    • Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin
    • Baum J, Dobson CM, Evans PA, Hanley C. 1989. Characterization of a partly folded protein by NMR methods: Studies on the molten globule state of guinea pig α-lactalbumin. Biochemistry 28:7-13.
    • (1989) Biochemistry , vol.28 , pp. 7-13
    • Baum, J.1    Dobson, C.M.2    Evans, P.A.3    Hanley, C.4
  • 10
    • 0016696854 scopus 로고
    • Modification of α-lactalbumin with N-bromosuccinimide and 2-hydroxy-5-nitrobenzylbromide
    • Bell JE, Castellino FJ, Trayer IP, Hill RL. 1975. Modification of α-lactalbumin with N-bromosuccinimide and 2-hydroxy-5-nitrobenzylbromide. J Biol Chem 250:7579-7585.
    • (1975) J Biol Chem , vol.250 , pp. 7579-7585
    • Bell, J.E.1    Castellino, F.J.2    Trayer, I.P.3    Hill, R.L.4
  • 11
    • 0023257088 scopus 로고
    • α-Lactalbumin binding to membranes: Evidence for a partially buried protein
    • Berliner LJ, Koga K. 1987. α-Lactalbumin binding to membranes: Evidence for a partially buried protein. Biochemistry 26:3006-3009.
    • (1987) Biochemistry , vol.26 , pp. 3006-3009
    • Berliner, L.J.1    Koga, K.2
  • 12
    • 0014216932 scopus 로고
    • Comparison of the amino acid sequence of bovine α-lactalbumin and hen's egg white lysozyme
    • Brew K, Vanaman TC, Hill RL. 1967. Comparison of the amino acid sequence of bovine α-lactalbumin and hen's egg white lysozyme. J Biol Chem 242:3747-3749.
    • (1967) J Biol Chem , vol.242 , pp. 3747-3749
    • Brew, K.1    Vanaman, T.C.2    Hill, R.L.3
  • 13
    • 0014010214 scopus 로고
    • Resolution of a soluble lactose synthetase into two protein components and solubilization of microsomal lactose synthetase
    • Brodbeck U, Ebner KE. 1966. Resolution of a soluble lactose synthetase into two protein components and solubilization of microsomal lactose synthetase. J Biol Chem 241:762-764.
    • (1966) J Biol Chem , vol.241 , pp. 762-764
    • Brodbeck, U.1    Ebner, K.E.2
  • 14
    • 0001055080 scopus 로고
    • Interactions of β-lactoglobulin and α-lactalbumin with lipids: A review
    • Brown EM. 1984. Interactions of β-lactoglobulin and α-lactalbumin with lipids: A review. J Dairy Sci 67:713-722.
    • (1984) J Dairy Sci , vol.67 , pp. 713-722
    • Brown, E.M.1
  • 15
    • 0014693695 scopus 로고
    • A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme
    • Browne WJ, North ACT, Phillips DC, Brew K, Vanaman TC, Hill RL. 1969. A possible three-dimensional structure of bovine α-lactalbumin based on that of hen's egg-white lysozyme. J Mol Biol 42:65-86.
    • (1969) J Mol Biol , vol.42 , pp. 65-86
    • Browne, W.J.1    North, A.C.T.2    Phillips, D.C.3    Brew, K.4    Vanaman, T.C.5    Hill, R.L.6
  • 16
    • 0017883676 scopus 로고
    • Relationship of thermal quenching of protein fluorescence to intramolecular structural mobility
    • Bushueva TL, Busel EP, Burstein EA. 1978. Relationship of thermal quenching of protein fluorescence to intramolecular structural mobility. Biochem Biophys Acta 534:141-152.
    • (1978) Biochem Biophys Acta , vol.534 , pp. 141-152
    • Bushueva, T.L.1    Busel, E.P.2    Burstein, E.A.3
  • 17
    • 0027280472 scopus 로고
    • Structure and stability of the molten globule state of guinea pig α-lactalbumin: A hydrogen exchange study
    • Chyan CL, Wormald C, Dobson CM, Evans P, Baum J. 1993. Structure and stability of the molten globule state of guinea pig α-lactalbumin: A hydrogen exchange study. Biochemistry 32:5681-5691.
    • (1993) Biochemistry , vol.32 , pp. 5681-5691
    • Chyan, C.L.1    Wormald, C.2    Dobson, C.M.3    Evans, P.4    Baum, J.5
  • 18
    • 0025179832 scopus 로고
    • Protein folding
    • Creighton TE. 1990. Protein folding. Biochem J 270:1-16.
    • (1990) Biochem J , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 20
    • 0020487551 scopus 로고
    • An intramolecular excimer-forming probe used to study the interaction of α-lactalbumin with model membranes
    • Dangreau H, Joniau M, DeCuyper M, Hanssens I. 1982. An intramolecular excimer-forming probe used to study the interaction of α-lactalbumin with model membranes. Biochemistry 21:3594-3598.
    • (1982) Biochemistry , vol.21 , pp. 3594-3598
    • Dangreau, H.1    Joniau, M.2    Decuyper, M.3    Hanssens, I.4
  • 22
    • 8944248548 scopus 로고
    • A biological role for α-lactalbumin as a component of an enzyme requiring two proteins
    • Ebner KE. 1970. A biological role for α-lactalbumin as a component of an enzyme requiring two proteins. Acc Chem Res 3:41-47.
    • (1970) Acc Chem Res , vol.3 , pp. 41-47
    • Ebner, K.E.1
  • 23
    • 0342640359 scopus 로고
    • Lactose synthetase
    • Ebner KE. 1973. Lactose synthetase. The Enzymes 9:363-377.
    • (1973) The Enzymes , vol.9 , pp. 363-377
    • Ebner, K.E.1
  • 24
    • 0002848296 scopus 로고
    • Fluorescence quenching reactions: Probing biological macromolecular structures
    • Dewey TG, ed. New York: Plenum
    • Eftink MR. 1991. Fluorescence quenching reactions: Probing biological macromolecular structures. In: Dewey TG, ed. Biophysical and biochemical aspects of fluorescence spectroscopy. New York: Plenum. pp 1-41.
    • (1991) Biophysical and Biochemical Aspects of Fluorescence Spectroscopy , pp. 1-41
    • Eftink, M.R.1
  • 25
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink MR. 1994. The use of fluorescence methods to monitor unfolding transitions in proteins Biophys J 66:482-501.
    • (1994) Biophys J , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 26
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies
    • Eftink MR, Ghiron CA. 1976. Exposure of tryptophanyl residues in proteins. Quantitative determination by fluorescence quenching studies. Biochemistry 15:672-680.
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 27
    • 0014808814 scopus 로고
    • Enzymic assay for galactosyl transferase activity of lactose synthetase and α-lactalbumin in purified and crude systems
    • Fitzgerald DK, Colvin B, Mawal R, Ebner KE. 1970. Enzymic assay for galactosyl transferase activity of lactose synthetase and α-lactalbumin in purified and crude systems. Anal Biochem 36:43-60.
    • (1970) Anal Biochem , vol.36 , pp. 43-60
    • Fitzgerald, D.K.1    Colvin, B.2    Mawal, R.3    Ebner, K.E.4
  • 28
    • 0001529088 scopus 로고
    • Quasielastic light scattering from human lactalbumin: Comparison of molecular dimensions in native and "molten globule" states
    • Gast K, Zirwer D, Welfe H, Bychkova VE, Ptitsyn OB. 1986. Quasielastic light scattering from human lactalbumin: Comparison of molecular dimensions in native and "molten globule" states. Int J Biol Macromol 8:231-236.
    • (1986) Int J Biol Macromol , vol.8 , pp. 231-236
    • Gast, K.1    Zirwer, D.2    Welfe, H.3    Bychkova, V.E.4    Ptitsyn, O.B.5
  • 29
    • 0028095491 scopus 로고
    • Study by mutagenesis of the roles of two aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system
    • Grobler JA, Wang M, Pike ACW, Brew K. 1994. Study by mutagenesis of the roles of two aromatic clusters of α-lactalbumin in aspects of its action in the lactose synthase system. J Biol Chem 269:5106-5114.
    • (1994) J Biol Chem , vol.269 , pp. 5106-5114
    • Grobler, J.A.1    Wang, M.2    Pike, A.C.W.3    Brew, K.4
  • 30
    • 0017877803 scopus 로고
    • Immobilized bovine lactose synthetase - A method of topographical analysis of the active site
    • Grunwald J, Berliner LJ. 1978. Immobilized bovine lactose synthetase - A method of topographical analysis of the active site. Biochim Biophys Acta 523:53-58.
    • (1978) Biochim Biophys Acta , vol.523 , pp. 53-58
    • Grunwald, J.1    Berliner, L.J.2
  • 31
    • 0021098342 scopus 로고
    • Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. III. Influence of the temperature and of the lipid-to-protein molar ratio on the complex formation
    • Hanssens I, Herreman W, Van Ceunebroeck JC, Dangreau H, Gielens C, Preaux G, Van Cauwelaert FH. 1983. Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. III. Influence of the temperature and of the lipid-to-protein molar ratio on the complex formation. Biochim Biophys Acta 728:293-304.
    • (1983) Biochim Biophys Acta , vol.728 , pp. 293-304
    • Hanssens, I.1    Herreman, W.2    Van Ceunebroeck, J.C.3    Dangreau, H.4    Gielens, C.5    Preaux, G.6    Van Cauwelaert, F.H.7
  • 32
    • 0019328332 scopus 로고
    • Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. I. A microcalorimetric and fluorescence study
    • Hanssens I, Houthuys C, Herreman W, Van Cauwelaert FH. 1980. Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. I. A microcalorimetric and fluorescence study. Biochim Biophys Acta 602:539-557.
    • (1980) Biochim Biophys Acta , vol.602 , pp. 539-557
    • Hanssens, I.1    Houthuys, C.2    Herreman, W.3    Van Cauwelaert, F.H.4
  • 33
    • 0021876398 scopus 로고
    • Influence of the protein conformation on the interaction between α-lactalbumin and dimyristoylphosphatidylcholine vesicles
    • Hanssens I, van Ceunebroeck JC, Pottel H, Preaux G, van Cauwelaert F. 1985. Influence of the protein conformation on the interaction between α-lactalbumin and dimyristoylphosphatidylcholine vesicles. Biochim Biophys Acta 817:154-166.
    • (1985) Biochim Biophys Acta , vol.817 , pp. 154-166
    • Hanssens, I.1    Van Ceunebroeck, J.C.2    Pottel, H.3    Preaux, G.4    Van Cauwelaert, F.5
  • 34
    • 8944242864 scopus 로고
    • Use of energy transfer to study the interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles
    • Herreman W, Van Cauwelaert F, Hanssens I. 1981a. Use of energy transfer to study the interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. Biochem International 2:237-242.
    • (1981) Biochem International , vol.2 , pp. 237-242
    • Herreman, W.1    Van Cauwelaert, F.2    Hanssens, I.3
  • 35
    • 0019886182 scopus 로고
    • Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. 11. A fluorescence polarization study
    • Herreman W, Van Turnout P, Van Cauwelaert FH, Hanssens I. 1981b. Interaction of α-lactalbumin with dimyristoyl phosphatidylcholine vesicles. 11. A fluorescence polarization study. Biochim Biophys Acta 640:419-429.
    • (1981) Biochim Biophys Acta , vol.640 , pp. 419-429
    • Herreman, W.1    Van Turnout, P.2    Van Cauwelaert, F.H.3    Hanssens, I.4
  • 38
    • 0014441009 scopus 로고
    • Studies on phosphatidylcholine vesicles. Formation and characteristics
    • Huang C. 1969. Studies on phosphatidylcholine vesicles. Formation and characteristics. Biochemistry 8:344-352.
    • (1969) Biochemistry , vol.8 , pp. 344-352
    • Huang, C.1
  • 39
    • 0016360614 scopus 로고
    • Preparation of homogeneous, single-walled phosphatidylcholine vesicles
    • Huang C, Thompson TE. 1970. Preparation of homogeneous, single-walled phosphatidylcholine vesicles. Methods Enzymol 32:485-489.
    • (1970) Methods Enzymol , vol.32 , pp. 485-489
    • Huang, C.1    Thompson, T.E.2
  • 40
    • 0022702283 scopus 로고
    • 2+-induced alteration in the unfolding behavior of α-lactalbumin
    • 2+-induced alteration in the unfolding behavior of α-lactalbumin. J Biochem 99:1191-1201.
    • (1986) J Biochem , vol.99 , pp. 1191-1201
    • Ikeguchi, M.1    Kuwajima, K.2    Sugai, S.3
  • 41
    • 0023040490 scopus 로고
    • Fusion of phospholipid vesicles induced by α-lactalbumin at acidic pH
    • Kim J, Kim H. 1986. Fusion of phospholipid vesicles induced by α-lactalbumin at acidic pH. Biochemistry 25:7867-7874.
    • (1986) Biochemistry , vol.25 , pp. 7867-7874
    • Kim, J.1    Kim, H.2
  • 42
    • 0001501418 scopus 로고
    • Inter- and intramolecular interactions of α-lactalbumin. 1. The apparent heterogeneity at acid pH
    • Kronman MJ, Andreotti RE. 1964. Inter- and intramolecular interactions of α-lactalbumin. 1. The apparent heterogeneity at acid pH. Biochemistry 3:1145-1151.
    • (1964) Biochemistry , vol.3 , pp. 1145-1151
    • Kronman, M.J.1    Andreotti, R.E.2
  • 43
    • 84981611610 scopus 로고
    • The fluorescence of native, denatured and reduced-denatured proteins
    • Kronman MJ, Holmes L. 1971. The fluorescence of native, denatured and reduced-denatured proteins. Photochemistry and Photobiology 14:113-134.
    • (1971) Photochemistry and Photobiology , vol.14 , pp. 113-134
    • Kronman, M.J.1    Holmes, L.2
  • 44
    • 0018977965 scopus 로고
    • Lactose synthesis: The possibilities of regulation
    • Kuhn NJ, Carrick DT, Wilde CJ. 1980. Lactose synthesis: The possibilities of regulation. J Dairy Sci 63:328-336.
    • (1980) J Dairy Sci , vol.63 , pp. 328-336
    • Kuhn, N.J.1    Carrick, D.T.2    Wilde, C.J.3
  • 45
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure
    • Kuwajima K. 1989. The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins Struct Funct Genet 6:87-103.
    • (1989) Proteins Struct Funct Genet , vol.6 , pp. 87-103
    • Kuwajima, K.1
  • 48
    • 0028811494 scopus 로고
    • Membrane-protein and the molten globule state - Interaction of α-lactalbumin with membranes
    • Lala AK, Kaul P, Ratnam PB. 1995. Membrane-protein and the molten globule state - Interaction of α-lactalbumin with membranes. J Protein Chem 14:601-609.
    • (1995) J Protein Chem , vol.14 , pp. 601-609
    • Lala, A.K.1    Kaul, P.2    Ratnam, P.B.3
  • 49
    • 0015230409 scopus 로고
    • Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion
    • Lehrer SS. 1971. Solute perturbation of protein fluorescence. The quenching of the tryptophyl fluorescence of model compounds and of lysozyme by iodide ion. Biochemistry 10:3254-3263.
    • (1971) Biochemistry , vol.10 , pp. 3254-3263
    • Lehrer, S.S.1
  • 50
    • 0023664860 scopus 로고
    • Spontaneous fusion of phosphatidylcholine small unilamellar vesicles in the fluid phase
    • Lentz BR, Carpenter TJ, Alford DR. 1987. Spontaneous fusion of phosphatidylcholine small unilamellar vesicles in the fluid phase. Biochemistry 26:5389-5397.
    • (1987) Biochemistry , vol.26 , pp. 5389-5397
    • Lentz, B.R.1    Carpenter, T.J.2    Alford, D.R.3
  • 51
    • 0021152966 scopus 로고
    • Metal-ion-dependent hydrophobic-interaction chromatography of α-lactalbumins
    • Lindahl L, Vogel HJ. 1984. Metal-ion-dependent hydrophobic-interaction chromatography of α-lactalbumins. Anal Biochem 140:394-402.
    • (1984) Anal Biochem , vol.140 , pp. 394-402
    • Lindahl, L.1    Vogel, H.J.2
  • 52
    • 0025811817 scopus 로고
    • Lysozyme and α-lactalbumin: Structure, function and interrelationships
    • McKenzie HA, White FH. 1991. Lysozyme and α-lactalbumin: Structure, function and interrelationships. Adv Protein Chem 41:173-315.
    • (1991) Adv Protein Chem , vol.41 , pp. 173-315
    • McKenzie, H.A.1    White, F.H.2
  • 53
    • 0027300005 scopus 로고
    • Relationship between annexin V tryptophan exposure, calcium and phospholipid binding
    • Meers P, Mealy T. 1993. Relationship between annexin V tryptophan exposure, calcium and phospholipid binding. Biochemistry 32:5411-5418.
    • (1993) Biochemistry , vol.32 , pp. 5411-5418
    • Meers, P.1    Mealy, T.2
  • 54
    • 0021112347 scopus 로고
    • Modulation of bovine milk galactosyltransferase activity by lipids
    • Mitranic MM, Boggs JM, Moscarello MA. 1983. Modulation of bovine milk galactosyltransferase activity by lipids. J Biol Chem 258:8630-8636.
    • (1983) J Biol Chem , vol.258 , pp. 8630-8636
    • Mitranic, M.M.1    Boggs, J.M.2    Moscarello, M.A.3
  • 55
    • 0021815347 scopus 로고
    • The effect of acidic lipids on the activity of bovine milk galactosyltransferase in vesicles of different phosphatidylethanolamines
    • Mitranic MM, Moscarello MA. 1985. The effect of acidic lipids on the activity of bovine milk galactosyltransferase in vesicles of different phosphatidylethanolamines. Biochim Biophys Acta 816:182-186.
    • (1985) Biochim Biophys Acta , vol.816 , pp. 182-186
    • Mitranic, M.M.1    Moscarello, M.A.2
  • 56
    • 0024285149 scopus 로고
    • The interaction of bovine milk galactosyltransferase with lipid and α-lactalbumin
    • Mitranic MM, Paquet MR, Moscarello MA. 1988. The interaction of bovine milk galactosyltransferase with lipid and α-lactalbumin. Biochim Biophys Acta 958:277-284.
    • (1988) Biochim Biophys Acta , vol.958 , pp. 277-284
    • Mitranic, M.M.1    Paquet, M.R.2    Moscarello, M.A.3
  • 57
    • 0020335465 scopus 로고
    • The binding of naphthalene dyes to the N and A conformers of bovine α-lactalbumin
    • Mulqueen PM, Kronman MJ. 1982. The binding of naphthalene dyes to the N and A conformers of bovine α-lactalbumin. Arch Biochem Biophys 215:28-39.
    • (1982) Arch Biochem Biophys , vol.215 , pp. 28-39
    • Mulqueen, P.M.1    Kronman, M.J.2
  • 59
    • 0021095471 scopus 로고
    • A distinct zinc binding site in the α-lactalbumins regulates calcium binding. Is there a physiological role for this control?
    • Murakami K, Berliner LJ. 1983. A distinct zinc binding site in the α-lactalbumins regulates calcium binding. Is there a physiological role for this control? Biochemistry 22:3370-3374.
    • (1983) Biochemistry , vol.22 , pp. 3370-3374
    • Murakami, K.1    Berliner, L.J.2
  • 60
    • 0022381730 scopus 로고
    • Probing different conformational states of bovine α-lactalbumin: Fluorescence studies with 4,4′-bis[1-(phenylamino)-8-naphthalenesulfonate]
    • Musci G, Berliner LJ. 1985a. Probing different conformational states of bovine α-lactalbumin: Fluorescence studies with 4,4′-bis[1-(phenylamino)-8-naphthalenesulfonate]. Biochemistry 24:3852-3856.
    • (1985) Biochemistry , vol.24 , pp. 3852-3856
    • Musci, G.1    Berliner, L.J.2
  • 61
    • 0022369894 scopus 로고
    • Physiological roles of zinc and calcium binding to α-lactalbumin in lactose biosynthesis
    • Musci G, Berliner LJ. 1985b. Physiological roles of zinc and calcium binding to α-lactalbumin in lactose biosynthesis. Biochemistry 24:6945-6948.
    • (1985) Biochemistry , vol.24 , pp. 6945-6948
    • Musci, G.1    Berliner, L.J.2
  • 62
    • 0022445298 scopus 로고
    • Cationic activation of galactosyltransferase from rat mammary golgi membranes by polyamines and by basic peptides and proteins
    • Navratnam N, Virk SS, Ward S, Kuhn NJ. 1986. Cationic activation of galactosyltransferase from rat mammary golgi membranes by polyamines and by basic peptides and proteins. Biochem J 239:423-433.
    • (1986) Biochem J , vol.239 , pp. 423-433
    • Navratnam, N.1    Virk, S.S.2    Ward, S.3    Kuhn, N.J.4
  • 63
    • 0023911121 scopus 로고
    • Purification, properties and cation activation of galactosyltransferase from lactating-rat mammary Golgi membranes
    • Navratnam N, Ward S, Fisher C, Kuhn NJ, Keen JN, Findlay JBC. 1988. Purification, properties and cation activation of galactosyltransferase from lactating-rat mammary Golgi membranes. J Biochem 171:623-629.
    • (1988) J Biochem , vol.171 , pp. 623-629
    • Navratnam, N.1    Ward, S.2    Fisher, C.3    Kuhn, N.J.4    Keen, J.N.5    Findlay, J.B.C.6
  • 65
    • 0021114569 scopus 로고
    • "Molten-globule state:" a compact form of globular proteins with mobile side-chains
    • Ohgushi M, Wada A. 1983. "Molten-globule state:" A compact form of globular proteins with mobile side-chains. FEBS Lett 164:21-24.
    • (1983) FEBS Lett , vol.164 , pp. 21-24
    • Ohgushi, M.1    Wada, A.2
  • 66
    • 0023938824 scopus 로고
    • Environment of tryptophan residues in various conformational states of α-lactalbumin studied by time-resolved and steady-state fluorescence spectroscopy
    • Ostrovsky AV, Kalinichenko LP, Emelyanenko VI, Klimanov AV, Permyakov EA. 1988. Environment of tryptophan residues in various conformational states of α-lactalbumin studied by time-resolved and steady-state fluorescence spectroscopy. Biophys Chem 30:105-115.
    • (1988) Biophys Chem , vol.30 , pp. 105-115
    • Ostrovsky, A.V.1    Kalinichenko, L.P.2    Emelyanenko, V.I.3    Klimanov, A.V.4    Permyakov, E.A.5
  • 68
    • 0021435096 scopus 로고
    • Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence
    • Permyakov EA, Burstein EA. 1984. Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence. Biophys Chem 19:265-271.
    • (1984) Biophys Chem , vol.19 , pp. 265-271
    • Permyakov, E.A.1    Burstein, E.A.2
  • 70
    • 0022760917 scopus 로고
    • 2+ content on the conformation of α-lactalbumin in a medium modelling physiological conditions
    • 2+ content on the conformation of α-lactalbumin in a medium modelling physiological conditions. Gen Physiol Biophys 5:377-390.
    • (1986) Gen Physiol Biophys , vol.5 , pp. 377-390
    • Permyakov, E.A.1    Kreimer, D.I.2
  • 71
    • 0023958674 scopus 로고
    • Interaction of calcium binding proteins, parvalbumin and α-lactalbumin, with dipalmitoyl-phosphatidylcholine vesicles
    • Permyakov EA, Kreimer DI, Kalinichenko LP, Shnyrov VL. 1988a. Interaction of calcium binding proteins, parvalbumin and α-lactalbumin, with dipalmitoyl-phosphatidylcholine vesicles. Gen Physiol Biophys 7:95-107.
    • (1988) Gen Physiol Biophys , vol.7 , pp. 95-107
    • Permyakov, E.A.1    Kreimer, D.I.2    Kalinichenko, L.P.3    Shnyrov, V.L.4
  • 72
    • 0021979565 scopus 로고
    • Cation binding effects on the pH, thermal and urea denaturations in α-lactalbumin
    • Permyakov EA, Morozova LA, Burstein EA. 1985. Cation binding effects on the pH, thermal and urea denaturations in α-lactalbumin. Biophys Chem 21:21-31.
    • (1985) Biophys Chem , vol.21 , pp. 21-31
    • Permyakov, E.A.1    Morozova, L.A.2    Burstein, E.A.3
  • 75
    • 0019880942 scopus 로고
    • Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes
    • Permyakov EA, Yarmolenko VV, Kalinichenko LP, Morozova LA, Burstein EA. 1981b. Calcium binding to α-lactalbumin: Structural rearrangement and association constant evaluation by means of intrinsic protein fluorescence changes. Biochem Biophys Res Commun 100:191-197.
    • (1981) Biochem Biophys Res Commun , vol.100 , pp. 191-197
    • Permyakov, E.A.1    Yarmolenko, V.V.2    Kalinichenko, L.P.3    Morozova, L.A.4    Burstein, E.A.5
  • 76
    • 0023644395 scopus 로고
    • Is the thermally denatured protein unfolded? the example of α-lactalbumin
    • Pfeil W. 1987. Is the thermally denatured protein unfolded? The example of α-lactalbumin. Biochim Biophys Acta 911:114-116.
    • (1987) Biochim Biophys Acta , vol.911 , pp. 114-116
    • Pfeil, W.1
  • 78
    • 0023626273 scopus 로고
    • Protein folding: Hypotheses and experiments
    • Ptitsyn O. 1987. Protein folding: Hypotheses and experiments. J Protein Chem 6:273-293.
    • (1987) J Protein Chem , vol.6 , pp. 273-293
    • Ptitsyn, O.1
  • 79
    • 0002940127 scopus 로고
    • The molten globule state
    • Creighton TE, ed. New York: Freeman
    • Ptitsyn O. 1992. The molten globule state. In: Creighton TE, ed. Protein folding. New York: Freeman, pp 243-300.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.1
  • 80
    • 0015502673 scopus 로고
    • A general strategy for parameter estimation from isosteric and allosteric-kinetic data and binding measurements
    • Reich JG, Wangermann G, Falck M, Rohde K. 1972. A general strategy for parameter estimation from isosteric and allosteric-kinetic data and binding measurements. Eur J Biochem 26:368-379.
    • (1972) Eur J Biochem , vol.26 , pp. 368-379
    • Reich, J.G.1    Wangermann, G.2    Falck, M.3    Rohde, K.4
  • 81
    • 0027220867 scopus 로고
    • α-Lactalbumin possesses a distinct zinc binding site
    • Ren J, Stuart DI, Acharya KR. 1993. α-Lactalbumin possesses a distinct zinc binding site J Biol Chem 268:19292-19298.
    • (1993) J Biol Chem , vol.268 , pp. 19292-19298
    • Ren, J.1    Stuart, D.I.2    Acharya, K.R.3
  • 82
    • 0019000261 scopus 로고
    • Comparative fluorescence properties of bovine, goat, human and guinea pig α-lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers
    • Sommers PB, Kronman MJ. 1980. Comparative fluorescence properties of bovine, goat, human and guinea pig α-lactalbumin. Characterization of the environments of individual tryptophan residues in partially folded conformers. Biophys Chem 11:217-232.
    • (1980) Biophys Chem , vol.11 , pp. 217-232
    • Sommers, P.B.1    Kronman, M.J.2
  • 84
    • 0028215584 scopus 로고
    • Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: Interfacial binding, catalysis and activation
    • Volwerk JJ, Filthruth E, Griffith OH, Jain MK. 1994. Phosphatidylinositol-specific phospholipase C from Bacillus cereus at the lipid-water interface: Interfacial binding, catalysis and activation. Biochemistry 33:3464-3474.
    • (1994) Biochemistry , vol.33 , pp. 3464-3474
    • Volwerk, J.J.1    Filthruth, E.2    Griffith, O.H.3    Jain, M.K.4
  • 85
    • 0025082341 scopus 로고
    • Divalent cation activation of galactosyltransferase in native mammary Golgi vesicles
    • Witsell DL, Casey CE, Neville MC. 1990. Divalent cation activation of galactosyltransferase in native mammary Golgi vesicles. J Biol Chem 265: 15731-15737.
    • (1990) J Biol Chem , vol.265 , pp. 15731-15737
    • Witsell, D.L.1    Casey, C.E.2    Neville, M.C.3
  • 86
    • 0026679847 scopus 로고
    • Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry
    • Yutani K, Ogasahara K, Kuwajima K. 1992. Absence of the thermal transition in apo-α-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry. J Mol Biol 228:347-350.
    • (1992) J Mol Biol , vol.228 , pp. 347-350
    • Yutani, K.1    Ogasahara, K.2    Kuwajima, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.