메뉴 건너뛰기




Volumn 69, Issue 10, 2005, Pages 1935-1943

Structural stabilities of recombinant scombridae fish myoglobins

Author keywords

Fish; Myoglobin; Recombinant; Stability

Indexed keywords

CHEMICAL MODIFICATION; ESCHERICHIA COLI; MUSCLE; MUTAGENESIS; THERMAL EFFECTS;

EID: 27644460437     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.69.1935     Document Type: Article
Times cited : (16)

References (34)
  • 2
    • 0038853525 scopus 로고    scopus 로고
    • Crystal structures of myoglobin-ligand complexes at near-atomic resolution
    • Vojtechovsky, J., Chu, K., Berendzen, J., Sweet, R. M., and Schlichting, I., Crystal structures of myoglobin-ligand complexes at near-atomic resolution. Biophys. J., 77, 2153-2174 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 2153-2174
    • Vojtechovsky, J.1    Chu, K.2    Berendzen, J.3    Sweet, R.M.4    Schlichting, I.5
  • 3
    • 0017112522 scopus 로고
    • Yellowfin tuna (Thunnus albacares) myoglobin: Characterization and comparative stability
    • Fosmire, G. J., and Brown, W. D., Yellowfin tuna (Thunnus albacares) myoglobin: characterization and comparative stability. Comp. Biochem. Physiol., 55B, 293-299 (1976).
    • (1976) Comp. Biochem. Physiol. , vol.55 B , pp. 293-299
    • Fosmire, G.J.1    Brown, W.D.2
  • 4
    • 0027974386 scopus 로고
    • 1.70 Å resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix
    • Birnbaum, G. I., Evans, S. V., Przybylska, M., and Rose, D. R., 1.70 Å resolution structure of myoglobin from yellowfin tuna. An example of a myoglobin lacking the D helix. Acta Cryst., D50, 283-289 (1994).
    • (1994) Acta Cryst. , vol.D50 , pp. 283-289
    • Birnbaum, G.I.1    Evans, S.V.2    Przybylska, M.3    Rose, D.R.4
  • 5
    • 0000605832 scopus 로고
    • Effect of freezing and thawing on the discoloration of tuna meat
    • Chow, C. J., Ochiai, Y., Watabe, S., and Hashimoto, K., Effect of freezing and thawing on the discoloration of tuna meat. Nippon Suisan Gakkaishi, 54, 639-648 (1988).
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 639-648
    • Chow, C.J.1    Ochiai, Y.2    Watabe, S.3    Hashimoto, K.4
  • 6
    • 0000213009 scopus 로고
    • Evaluation of tuna meat discoloration by Hunter color difference scale
    • Ochiai, Y., Chow, C. J., Watabe, S., and Hashimoto, K., Evaluation of tuna meat discoloration by Hunter color difference scale. Nippon Suisan Gakkaishi, 54, 649-653 (1988).
    • (1988) Nippon Suisan Gakkaishi , vol.54 , pp. 649-653
    • Ochiai, Y.1    Chow, C.J.2    Watabe, S.3    Hashimoto, K.4
  • 7
    • 0037014283 scopus 로고    scopus 로고
    • Myoglobin-induced lipid oxidation. A review
    • Baron, C. P., and Andersen, H. J., Myoglobin-induced lipid oxidation. A review. J. Agric. Food Chem., 50, 3887-3897 (2002).
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 3887-3897
    • Baron, C.P.1    Andersen, H.J.2
  • 8
    • 0023100151 scopus 로고
    • Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins
    • Aojula, H. S., Wilson, M. T., and Morrison, I. E. G., Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins. Biochem. J., 243, 205-210 (1987).
    • (1987) Biochem. J. , vol.243 , pp. 205-210
    • Aojula, H.S.1    Wilson, M.T.2    Morrison, I.E.G.3
  • 10
    • 0020981508 scopus 로고
    • Structural and functional aspects of the heart ventricle myoglobin of bluefin tuna
    • Colonna, G., Irace, G., Bismuto, E., Servillo, L., and Balestrieri, C., Structural and functional aspects of the heart ventricle myoglobin of bluefin tuna. Comp. Biochem. Physiol., 76A, 481-485 (1983).
    • (1983) Comp. Biochem. Physiol. , vol.76 A , pp. 481-485
    • Colonna, G.1    Irace, G.2    Bismuto, E.3    Servillo, L.4    Balestrieri, C.5
  • 11
    • 0041975088 scopus 로고
    • Relationship between the stability and autoxidation of myoglobin
    • Chow, C. J., Relationship between the stability and autoxidation of myoglobin. J. Agric. Food Chem., 39, 22-26 (1991).
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 22-26
    • Chow, C.J.1
  • 12
    • 0011762658 scopus 로고    scopus 로고
    • Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence
    • Chanthai, S., Ogawa, M., Tamiya, T., and Tsuchiya, T., Studies on thermal denaturation of fish myoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence. Fish. Sci., 62, 927-932 (1996).
    • (1996) Fish. Sci. , vol.62 , pp. 927-932
    • Chanthai, S.1    Ogawa, M.2    Tamiya, T.3    Tsuchiya, T.4
  • 13
    • 0342382548 scopus 로고    scopus 로고
    • Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence
    • Chanthai, S., Ogawa, M., Tamiya, T., and Tsuchiya, T., Studies on thermal denaturation of fish apomyoglobins using differential scanning calorimetry, circular dichroism, and tryptophan fluorescence. Fish. Sci., 62, 933-937 (1996).
    • (1996) Fish. Sci. , vol.62 , pp. 933-937
    • Chanthai, S.1    Ogawa, M.2    Tamiya, T.3    Tsuchiya, T.4
  • 15
    • 4644265549 scopus 로고
    • The concentration of myoglobin and hemoglobin in tuna flesh
    • Brown, W. D., The concentration of myoglobin and hemoglobin in tuna flesh. J. Food Sci., 27, 26-28 (1962).
    • (1962) J. Food Sci. , vol.27 , pp. 26-28
    • Brown, W.D.1
  • 16
    • 85007901041 scopus 로고
    • Chemical studies on the red muscle ("chiai") of fishes-II. Determinations of the content of hemoglobin, myoglobin and cytochrome c in the muscles of fishes
    • Matsuura, F., and Hashimoto, K., Chemical studies on the red muscle ("chiai") of fishes-II. Determinations of the content of hemoglobin, myoglobin and cytochrome c in the muscles of fishes. Bull. Japan. Soc. Sci. Fish., 20, 308-312 (1954).
    • (1954) Bull. Japan. Soc. Sci. Fish. , vol.20 , pp. 308-312
    • Matsuura, F.1    Hashimoto, K.2
  • 17
    • 85007875143 scopus 로고
    • Chemical studies on the red muscle ("chiai") of fishes-X. A new method for determination of myoglobin
    • Matsuura, F., and Hashimoto, K., Chemical studies on the red muscle ("chiai") of fishes-X. A new method for determination of myoglobin. Bull. Japan. Soc. Sci. Fish., 24, 809-815 (1959).
    • (1959) Bull. Japan. Soc. Sci. Fish. , vol.24 , pp. 809-815
    • Matsuura, F.1    Hashimoto, K.2
  • 18
    • 7544236251 scopus 로고    scopus 로고
    • Primary structure and thermostability of bigeye tuna myoglobin in relation to those from other scombridae fish
    • Ueki, N., and Ochiai, Y., Primary structure and thermostability of bigeye tuna myoglobin in relation to those from other scombridae fish. Fish. Sci., 70, 875-884 (2004).
    • (2004) Fish. Sci. , vol.70 , pp. 875-884
    • Ueki, N.1    Ochiai, Y.2
  • 19
    • 21644436544 scopus 로고    scopus 로고
    • Characterization of bullet tuna myoglobin with reference to thermostability-structure relationship
    • Ueki, N., Chow, C. J., and Ochiai, Y., Characterization of bullet tuna myoglobin with reference to thermostability-structure relationship. J. Agric. Food Chem., 53, 4968-4975 (2005).
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 4968-4975
    • Ueki, N.1    Chow, C.J.2    Ochiai, Y.3
  • 20
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in Escherichia coli
    • Springer, B. A., and Sligar, S. G., High-level expression of sperm whale myoglobin in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A., 84, 8961-8965 (1987).
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 21
    • 0022339199 scopus 로고
    • Cloning, expression in Escherichia coli, and reconstitution of human myoglobin
    • Varadarajan, R., Szabo, A., and Boxer, S. G., Cloning, expression in Escherichia coli, and reconstitution of human myoglobin. Proc. Natl. Acad. Sci. U.S.A., 82, 5681-5684 (1985).
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 5681-5684
    • Varadarajan, R.1    Szabo, A.2    Boxer, S.G.3
  • 22
    • 0035324637 scopus 로고    scopus 로고
    • How Ala→Gly mutations in different helices affect the stability of the apomyoglobin molten globule
    • Luo, Y., and Baldwin, R. L., How Ala→Gly mutations in different helices affect the stability of the apomyoglobin molten globule. Biochemistry, 40, 5283-5289 (2001).
    • (2001) Biochemistry , vol.40 , pp. 5283-5289
    • Luo, Y.1    Baldwin, R.L.2
  • 23
    • 14644415062 scopus 로고    scopus 로고
    • Autoreduction of ferryl myoglobin: Discrimination among the three tyrosine and two tryptophan residues as electron donors
    • Lardinois, O. M., and Montellao, P. R. O., Autoreduction of ferryl myoglobin: discrimination among the three tyrosine and two tryptophan residues as electron donors. Biochemistry, 43, 4601-4610 (2004).
    • (2004) Biochemistry , vol.43 , pp. 4601-4610
    • Lardinois, O.M.1    Montellao, P.R.O.2
  • 24
    • 0242321015 scopus 로고    scopus 로고
    • Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions
    • Nishimura, C., Wright, P. E., and Dyson, H. J., Role of the B helix in early folding events in apomyoglobin: evidence from site-directed mutagenesis for native-like long range interactions. J. Mol. Biol., 334, 293-307 (2003).
    • (2003) J. Mol. Biol. , vol.334 , pp. 293-307
    • Nishimura, C.1    Wright, P.E.2    Dyson, H.J.3
  • 26
    • 0346096857 scopus 로고    scopus 로고
    • Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins
    • Musto, R., Bigotti, M. G., Travaglini-Allocatelli, C., Brunori, M., and Cutruzzola, F., Folding of Aplysia limacina apomyoglobin involves an intermediate in common with other evolutionarily distant globins. Biochemistry, 43, 230-236 (2004).
    • (2004) Biochemistry , vol.43 , pp. 230-236
    • Musto, R.1    Bigotti, M.G.2    Travaglini-Allocatelli, C.3    Brunori, M.4    Cutruzzola, F.5
  • 27
    • 0022503457 scopus 로고
    • Calculation of protein concentration from circular dichroism
    • Yang, J. T., Wu, C.-S. C., and Martinez, H. M., Calculation of protein concentration from circular dichroism. Methods Enzymol., 130, 208-269 (1986).
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 28
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res., 22, 4673-4680 (1994).
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0037358773 scopus 로고    scopus 로고
    • Fast purification of the apo form and of a non-binding heme mutant of recombinant sperm whale myoglobin
    • Ribeiro, E. A. Jr., Regis, W. C. B., Tasic, L., and Ramos, C. H. I., Fast purification of the apo form and of a non-binding heme mutant of recombinant sperm whale myoglobin. Protein Express. Purif., 28, 202-208 (2003).
    • (2003) Protein Express. Purif. , vol.28 , pp. 202-208
    • Ribeiro Jr., E.A.1    Regis, W.C.B.2    Tasic, L.3    Ramos, C.H.I.4
  • 32
    • 0000686117 scopus 로고
    • Relative conformations of sperm whale metmyoglobin and apomyoglobin in solution
    • Breslow, E., Beychok, S., Hardman, K. D., and Gurd, F. R. N., Relative conformations of sperm whale metmyoglobin and apomyoglobin in solution. J. Biol. Chem., 240, 304-309 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 304-309
    • Breslow, E.1    Beychok, S.2    Hardman, K.D.3    Gurd, F.R.N.4
  • 34
    • 0028290594 scopus 로고
    • Acid-induced folding of heme proteins
    • Goto, Y., and Fink, A. L., Acid-induced folding of heme proteins. Methods Enzymol., 232, 3-15 (1994).
    • (1994) Methods Enzymol. , vol.232 , pp. 3-15
    • Goto, Y.1    Fink, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.