메뉴 건너뛰기




Volumn 67, Issue 4, 2003, Pages 830-837

Thermostabilization of Ovalbumin by an Alkaline Treatment: Examination for the Possible Implications of an Altered Serpin Loop Structure

Author keywords

Loop insertion; Ovalbumin; S ovalbumin; Serpin

Indexed keywords

INSERTION SEQUENCES;

EID: 0042821588     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.830     Document Type: Article
Times cited : (7)

References (35)
  • 1
    • 0027633477 scopus 로고
    • The role of conformational change in serpin structure and function
    • Gettins, P. E. W., Patston, P. A., and Schapira, M., The role of conformational change in serpin structure and function. BioEssays, 15, 461-467 (1993).
    • (1993) Bioessays , vol.15 , pp. 461-467
    • Gettins, P.E.W.1    Patston, P.A.2    Schapira, M.3
  • 2
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington, J. A., Read, R. J., and Carrell, R. W., Structure of a serpin-protease complex shows inhibition by deformation. Nature, 407, 923-926 (2000).
    • (2000) Nature , vol.407 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 3
    • 0024430428 scopus 로고
    • Ovalbumin and angiotensinogen lack serpin S-R conformational change
    • Stein, P. E., Tewkesbury, D. A., and Carrell, R. W., Ovalbumin and angiotensinogen lack serpin S-R conformational change. Biochem. J., 262, 103-107 (1989).
    • (1989) Biochem. J. , vol.262 , pp. 103-107
    • Stein, P.E.1    Tewkesbury, D.A.2    Carrell, R.W.3
  • 4
    • 0024557050 scopus 로고
    • Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin
    • Gettins, P., Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin. J. Biol. Chem., 264, 3781-3785 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 3781-3785
    • Gettins, P.1
  • 5
    • 0033837714 scopus 로고    scopus 로고
    • Bypassing the kinetic trap of serpin protein folding by loop extension
    • Im, H., Ahn, H. E., and Yu, M. H., Bypassing the kinetic trap of serpin protein folding by loop extension. Protein Science, 9, 1497-1502 (2000).
    • (2000) Protein Science , vol.9 , pp. 1497-1502
    • Im, H.1    Ahn, H.E.2    Yu, M.H.3
  • 6
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of ai-antitrypsin for structure and function of serpins
    • Huber, R., and Carrell, R. W., Implications of the three-dimensional structure of ai-antitrypsin for structure and function of serpins. Biochemistry, 28, 8951-8966 (1989).
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 7
    • 0032006633 scopus 로고    scopus 로고
    • An atlas of serpin conformations
    • Whisstock, J., Skinner, R., and Lesk, A. M., An atlas of serpin conformations. FEBSLett., 23, 63-67 (1998).
    • (1998) Febslett. , vol.23 , pp. 63-67
    • Whisstock, J.1    Skinner, R.2    Lesk, A.M.3
  • 8
    • 0021711639 scopus 로고
    • Ovalbumin is an elastase substrate
    • Wright, H.T., Ovalbumin is an elastase substrate. J. Biol. Chem., 259, 14335-14336 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 14335-14336
    • Wright, H.T.1
  • 9
    • 0025276661 scopus 로고
    • Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin
    • Wright, H. T., Qian, H. X., and Huber, R., Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin. J. Mol. Biol., 213, 513-528 (1990).
    • (1990) J. Mol. Biol. , vol.213 , pp. 513-528
    • Wright, H.T.1    Qian, H.X.2    Huber, R.3
  • 10
    • 0036298517 scopus 로고    scopus 로고
    • Loop-inserted and thermostabilized structure of P1-P1? Cleaved ovalbumin mutant R339T
    • Yamasaki, M., Arii, Y., Mikami, B., and Hirose, M., Loop-inserted and thermostabilized structure of P1-P1? cleaved ovalbumin mutant R339T. J. Mol. Biol., 307, 113-120 (2002).
    • (2002) J. Mol. Biol. , vol.307 , pp. 113-120
    • Yamasaki, M.1    Arii, Y.2    Mikami, B.3    Hirose, M.4
  • 11
    • 85010534323 scopus 로고
    • Modification of ovalbumin in stored eggs detected by heat denaturation
    • Smith, M. B., and Back, J. F., Modification of ovalbumin in stored eggs detected by heat denaturation. Nature, 18, 365-377 (1962).
    • (1962) Nature , vol.18 , pp. 365-377
    • Smith, M.B.1    Back, J.F.2
  • 12
    • 0001352497 scopus 로고
    • Studies on ovalbumin II. The formation and properties of S-ovalbumin, a more stable form of ovalbumin
    • Smith, M. B., and Back, J. F., Studies on ovalbumin II. The formation and properties of S-ovalbumin, a more stable form of ovalbumin. Aust. J. Biol. Sci., 18, 365-377 (1965).
    • (1965) Aust. J. Biol. Sci. , vol.18 , pp. 365-377
    • Smith, M.B.1    Back, J.F.2
  • 13
    • 0033574609 scopus 로고    scopus 로고
    • Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability
    • Sugimoto, Y., Sanuki, S., Ohsako, S., Higashimoto, Y., Kondo, M., Kurawaki, J., Ibrahim, H. R., Aoki, T., Kusakabe, T., and Koga, K., Ovalbumin in developing chicken eggs migrates from egg white to embryonic organs while changing its conformation and thermal stability. J. Biol. Chem., 274, 11030-11037 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 11030-11037
    • Sugimoto, Y.1    Sanuki, S.2    Ohsako, S.3    Higashimoto, Y.4    Kondo, M.5    Kurawaki, J.6    Ibrahim, H.R.7    Aoki, T.8    Kusakabe, T.9    Koga, K.10
  • 14
    • 0035463269 scopus 로고    scopus 로고
    • Thermostabilization of ovalbumin in a developing egg by an alkalinity-regulated, two-step process
    • Hatta, H., Nomura, M., Takahashi, N., and Hirose, M., Thermostabilization of ovalbumin in a developing egg by an alkalinity-regulated, two-step process. Biosci. Biotechnol. Biochem., 65, 2021-2027 (2001).
    • (2001) Biosci. Biotechnol. Biochem. , vol.65 , pp. 2021-2027
    • Hatta, H.1    Nomura, M.2    Takahashi, N.3    Hirose, M.4
  • 15
    • 0000315612 scopus 로고
    • Changes of the heat-induced gelling properties of ovalbumin during its conversion to S-ovalbumin
    • Shitamori, S., Kojima, E., and Nakamura, R., Changes of the heat-induced gelling properties of ovalbumin during its conversion to S-ovalbumin. Agric. Biol. Chem., 48, 1539-1544 (1984).
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1539-1544
    • Shitamori, S.1    Kojima, E.2    Nakamura, R.3
  • 16
    • 0016923455 scopus 로고
    • A differential scanning calorimetric study of conversion of ovalbumin to S-ovalbumin in eggs
    • Donovan, J. W., and Mapes, C. J., A differential scanning calorimetric study of conversion of ovalbumin to S-ovalbumin in eggs. J. Sci. Fd. Agric., 27, 197-204 (1976).
    • (1976) J. Sci. Fd. Agric. , vol.27 , pp. 197-204
    • Donovan, J.W.1    Mapes, C.J.2
  • 17
    • 0028945610 scopus 로고
    • S-ovalbumin, an ovalbumin conformer with properties analogous to those of loop-inserted serpins
    • Huntington, J. A., Patston, P. A., and Gettins, P. G. W., S-ovalbumin, an ovalbumin conformer with properties analogous to those of loop-inserted serpins. Protein Sci., 4, 613-621 (1995).
    • (1995) Protein Sci. , vol.4 , pp. 613-621
    • Huntington, J.A.1    Patston, P.A.2    Gettins, P.G.W.3
  • 18
    • 0035947059 scopus 로고    scopus 로고
    • Structure and properties of ovalbumin
    • Hungtington, J. A., and Stein, P. E., Structure and properties of ovalbumin. J. Chromatography B, 756, 189-198 (2001).
    • (2001) J. Chromatography B , vol.756 , pp. 189-198
    • Hungtington, J.A.1    Stein, P.E.2
  • 19
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell, R.W., Evans, D. L. I., and Stein, P. E., Mobile reactive centre of serpins and the control of thrombosis. Nature, 353, 576-578 (1991).
    • (1991) Nature , vol.353 , pp. 576-578
    • Carrell, R.W.1    Evans, D.L.I.2    Stein, P.E.3
  • 20
    • 0028773279 scopus 로고
    • Biological implications of a 3 A structure of dimeric antithrombin
    • Carrell, R. W., Stein, P. E., Fermi, G., and Wardell, R., Biological implications of a 3 A structure of dimeric antithrombin. Structure, 2, 257-270 (1994).
    • (1994) Structure , vol.2 , pp. 257-270
    • Carrell, R.W.1    Stein, P.E.2    Fermi, G.3    Wardell, R.4
  • 21
    • 0042852414 scopus 로고
    • Studies on proteins. 1. On the preparation of egg-albumin solutions of well-defined composition, and on the analytical methods used
    • Sorensen, S. P. L., and Hoyrup, M., Studies on proteins. 1. On the preparation of egg-albumin solutions of well-defined composition, and on the analytical methods used. C. R. Lab. Carlsberg Ser. Chim., 12, 12-67 (1915-1917).
    • (1915) C. R. Lab. Carlsberg Ser. Chim , vol.12 , pp. 12-67
    • Sorensen, S.P.L.1    Hoyrup, M.2
  • 22
    • 85004367709 scopus 로고
    • Physicochemical and functional properties of hen ovalbumin dephosphorylated by acid phosphatase
    • Kitabatake, N., Ishida, A., and Doi, E., Physicochemical and functional properties of hen ovalbumin dephosphorylated by acid phosphatase. Agric. Biol. Chem., 52, 967-973 (1988).
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 967-973
    • Kitabatake, N.1    Ishida, A.2    Doi, E.3
  • 23
    • 78651036085 scopus 로고
    • The transformation of ovalbumin into plakalbumin: A case of limited proteolysis
    • Ottesen, M., The transformation of ovalbumin into plakalbumin: A case of limited proteolysis. C. R. Lab. Carlsberg Ser. Chim., 30, 211-270 (1958).
    • (1958) C. R. Lab. Carlsberg Ser. Chim. , vol.30 , pp. 211-270
    • Ottesen, M.1
  • 24
    • 0033176603 scopus 로고    scopus 로고
    • Structural properties of recombinant ovalbumin and its transformation into a thermostabilized form by alkaline treatment
    • Arii, Y., Takahashi, N., Tatsumi, E., and Hirose, M., Structural properties of recombinant ovalbumin and its transformation into a thermostabilized form by alkaline treatment. Biosci. Biotechnol. Biochem., 63, 1392-1399 (1999).
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 1392-1399
    • Arii, Y.1    Takahashi, N.2    Tatsumi, E.3    Hirose, M.4
  • 25
    • 0037090807 scopus 로고    scopus 로고
    • Probing the serpin structural transition mechanism in an ovalbumin mutant R339T by proteolytic cleavage kinetics of the reactive center loop
    • Arii, Y., and Hirose, M., Probing the serpin structural transition mechanism in an ovalbumin mutant R339T by proteolytic cleavage kinetics of the reactive center loop. Biochem. J., 363, 403-409 (2002).
    • (2002) Biochem. J. , vol.363 , pp. 403-409
    • Arii, Y.1    Hirose, M.2
  • 26
    • 0000629760 scopus 로고
    • The denaturation of proteins II. Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution
    • Glazer, A. N., Mckenzie, H. A., and Wake, R. G., The denaturation of proteins II. Ultraviolet absorption spectra of bovine serum albumin and ovalbumin in urea and in acid solution. Biochim. Biophys. Acta, 69, 240-248 (1963).
    • (1963) Biochim. Biophys. Acta , vol.69 , pp. 240-248
    • Glazer, A.N.1    Mc Kenzie, H.A.2    Wake, R.G.3
  • 27
    • 0021747157 scopus 로고
    • Human arproteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • rproteinase inhibitor: Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J. Mol. Biol., 177, 531-556 (1984).
    • (1984) J. Mol. Biol. , vol.177 , pp. 531-556
    • Loebermann, H.1    Tokuoka, R.2    Deisenhofer, J.3    Huber, R.4
  • 28
    • 0000978913 scopus 로고
    • Plakalbumin converts to heat-stable form under the condition as ovalbumin-S-ovalbumin transformation
    • Shitamori, S., and Nakamura, R., Plakalbumin converts to heat-stable form under the condition as ovalbumin-S-ovalbumin transformation. J. Agric. Food Chem., 31, 513-516 (1983).
    • (1983) J. Agric. Food Chem. , vol.31 , pp. 513-516
    • Shitamori, S.1    Nakamura, R.2
  • 30
    • 0024557050 scopus 로고
    • Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin
    • Gettins, P. G. W., Absence of large-scale conformational change upon limited proteolysis of ovalbumin, the prototypic serpin. J. Biol. Chem., 264, 3781-3785 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 3781-3785
    • Gettins, P.G.W.1
  • 31
    • 4544369373 scopus 로고
    • The specificities of chicken ovomucoid and ovoinhibitor
    • Feeney, R. E., Stevens, F. C., and Osuga, D. T., The specificities of chicken ovomucoid and ovoinhibitor. J. Biol. Chem., 238, 1415-1418 (1963).
    • (1963) J. Biol. Chem. , vol.238 , pp. 1415-1418
    • Feeney, R.E.1    Stevens, F.C.2    Osuga, D.T.3
  • 32
    • 0004899298 scopus 로고
    • Liberation of carboxyl groups on conversion of ovalbumin to S-ovalbumin
    • Nakamura, R., Takemori, J., and Shitamori, S., Liberation of carboxyl groups on conversion of ovalbumin to S-ovalbumin. Agric. Biol. Chem., 45, 1653-1659 (1981).
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 1653-1659
    • Nakamura, R.1    Takemori, J.2    Shitamori, S.3
  • 33
    • 85009635721 scopus 로고
    • Deamidation of ovalbumin during S-ovalbumin conversion
    • Kato, A., Tanaka, A., Matsudomi, N., and Kobayashi, K., Deamidation of ovalbumin during S-ovalbumin conversion. Agric. Biol. Chem., 50, 2375-2376 (1986).
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 2375-2376
    • Kato, A.1    Tanaka, A.2    Matsudomi, N.3    Kobayashi, K.4
  • 34
    • 84985666817 scopus 로고
    • A Raman difference spectroscopic investigation of ovalbumin and S-oval-bumin
    • Kint, S., and Tomimatsu, Y., A Raman difference spectroscopic investigation of ovalbumin and S-oval-bumin. Biopolymers, 18, 1073-1079 (1979).
    • (1979) Biopolymers , vol.18 , pp. 1073-1079
    • Kint, S.1    Tomimatsu, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.