메뉴 건너뛰기




Volumn 80, Issue 1, 1999, Pages 21-30

Temperature and domain size dependence of sickle cell hemoglobin polymer melting in high concentration phosphate buffer

Author keywords

Depolymerization; Domain size; Kinetics; Melting; Sickle cell hemoglobin; Temperature

Indexed keywords

CARBON MONOXIDE; HEMOGLOBIN S;

EID: 0033584219     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(99)00056-3     Document Type: Article
Times cited : (9)

References (21)
  • 1
    • 0000420850 scopus 로고
    • A specific chemical difference between the globins of normal human and sickle cell anemia haemoglobin
    • Ingram V.M. A specific chemical difference between the globins of normal human and sickle cell anemia haemoglobin. Nature. 178:1956;792.
    • (1956) Nature , vol.178 , pp. 792
    • Ingram, V.M.1
  • 3
    • 0022253394 scopus 로고
    • Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal
    • Padlan E.A., Love W.E. Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal. J. Biol. Chem. 260:1985;8280.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8280
    • Padlan, E.A.1    Love, W.E.2
  • 4
    • 0023195612 scopus 로고
    • Delay time of hemoglobin S gelation prevents most cells from sickling in vivo
    • Mozzarelli A., Hofrichter J., Eaton W.A. Delay time of hemoglobin S gelation prevents most cells from sickling in vivo. Science. 237:1987;500.
    • (1987) Science , vol.237 , pp. 500
    • Mozzarelli, A.1    Hofrichter, J.2    Eaton, W.A.3
  • 5
    • 0021815445 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. I. Studies using temperature jump and laser photolysis techniques
    • Ferrone F.A., Hofrichter J., Eaton W.A. Kinetics of sickle hemoglobin polymerization. I. Studies using temperature jump and laser photolysis techniques. J. Mol. Biol. 183:1985;591.
    • (1985) J. Mol. Biol. , vol.183 , pp. 591
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 6
    • 0021837479 scopus 로고
    • Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism
    • Ferrone F.A., Hofrichter J., Eaton W.A. Kinetics of sickle hemoglobin polymerization. II. A double nucleation mechanism. J. Mol. Biol. 183:1985;611.
    • (1985) J. Mol. Biol. , vol.183 , pp. 611
    • Ferrone, F.A.1    Hofrichter, J.2    Eaton, W.A.3
  • 8
    • 0016294907 scopus 로고
    • The rates of polymerization and depolymerization of sickle cell hemoglobin
    • Moffat K., Gibson Q.H. The rates of polymerization and depolymerization of sickle cell hemoglobin. Biochem. Biophys. Res. Commun. 61:1974;237.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , pp. 237
    • Moffat, K.1    Gibson, Q.H.2
  • 10
    • 0028920158 scopus 로고
    • Nucleation fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels
    • Briehl R.W. Nucleation fiber growth and melting, and domain formation and structure in sickle cell hemoglobin gels. J. Mol. Biol. 245:1995;710.
    • (1995) J. Mol. Biol. , vol.245 , pp. 710
    • Briehl, R.W.1
  • 11
    • 0033024296 scopus 로고    scopus 로고
    • Sickle hemoglobin polymer melting in high concentration phosphate buffer
    • Louderback J.G., Ballas S.K., Kim-Shapiro D.B. Sickle hemoglobin polymer melting in high concentration phosphate buffer. Biophys. J. 76:1999;2216.
    • (1999) Biophys. J. , vol.76 , pp. 2216
    • Louderback, J.G.1    Ballas, S.K.2    Kim-Shapiro, D.B.3
  • 12
    • 0018679997 scopus 로고
    • Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations
    • Adachi K., Asukura T. Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations. J. Biol. Chem. 254:1979;7765.
    • (1979) J. Biol. Chem. , vol.254 , pp. 7765
    • Adachi, K.1    Asukura, T.2
  • 13
    • 0019429816 scopus 로고
    • Aggregation and crystallization of hemoglobins A, C and S. Probable formation of different nuclei for gelation and crystallization
    • Adachi K., Asukura T. Aggregation and crystallization of hemoglobins A, C and S. Probable formation of different nuclei for gelation and crystallization. J. Biol. Chem. 254:1981;1824.
    • (1981) J. Biol. Chem. , vol.254 , pp. 1824
    • Adachi, K.1    Asukura, T.2
  • 14
    • 0000041480 scopus 로고    scopus 로고
    • Polymerization of deoxy-sickle hemoglobin in high phosphate buffer
    • Wang Z.P., Chen Y.M., Josephs R. Polymerization of deoxy-sickle hemoglobin in high phosphate buffer. Biophys. J. 70:1996;435.
    • (1996) Biophys. J. , vol.70 , pp. 435
    • Wang, Z.P.1    Chen, Y.M.2    Josephs, R.3
  • 15
    • 0014670514 scopus 로고
    • Preparation and properties of α- and β-chains from human hemoglobin
    • Geraci G., Parkhurst L.J., Gibson Q.H. Preparation and properties of α- and β-chains from human hemoglobin. J. Biol. Chem. 17:1969;4664.
    • (1969) J. Biol. Chem. , vol.17 , pp. 4664
    • Geraci, G.1    Parkhurst, L.J.2    Gibson, Q.H.3
  • 16
    • 33747738463 scopus 로고
    • Singular value decomposition and least squares solutions
    • Golub G.H., Reinsch C. Singular value decomposition and least squares solutions. Numer. Math. 14:1970;403.
    • (1970) Numer. Math. , vol.14 , pp. 403
    • Golub, G.H.1    Reinsch, C.2
  • 17
    • 0026633609 scopus 로고
    • Singular value decomposition: Applications to experimental data
    • Henry E.R., Hofrichter J. Singular value decomposition: applications to experimental data. Methods Enzymol. 210:1992;129.
    • (1992) Methods Enzymol. , vol.210 , pp. 129
    • Henry, E.R.1    Hofrichter, J.2
  • 19
    • 0017667829 scopus 로고
    • Thermodynamics of gelation of sickle cell deoxyhemoglobin
    • Ross P.D., Hofrichter J., Eaton W.A. Thermodynamics of gelation of sickle cell deoxyhemoglobin. J. Mol. Biol. 115:1977;111.
    • (1977) J. Mol. Biol. , vol.115 , pp. 111
    • Ross, P.D.1    Hofrichter, J.2    Eaton, W.A.3
  • 20
    • 0020397654 scopus 로고
    • Kinetics of the polymerization of hemoglobin in high and low phosphate buffers
    • Adachi K., Asakura T. Kinetics of the polymerization of hemoglobin in high and low phosphate buffers. Blood Cells. 8:1982;213.
    • (1982) Blood Cells , vol.8 , pp. 213
    • Adachi, K.1    Asakura, T.2
  • 21
    • 0028063809 scopus 로고
    • Nanosecond absorption study of kinetics associated with carbon monoxide rebinding to hemoglobin S and hemoglobin C following laser photolysis
    • Shapiro D.B., Paquette S.J., Esquerra R.M. et al. Nanosecond absorption study of kinetics associated with carbon monoxide rebinding to hemoglobin S and hemoglobin C following laser photolysis. Biochem. Biophys. Res. Commun. 205:1994;154.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 154
    • Shapiro, D.B.1    Paquette, S.J.2    Esquerra, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.