메뉴 건너뛰기




Volumn 87, Issue 9, 1998, Pages 1062-1068

Effects of tween 80 and sucrose on acute short-term stability and long- term storage at -20 °C of a recombinant hemoglobin

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN DERIVATIVE; POLYSORBATE 80; RECOMBINANT PROTEIN; SUCROSE;

EID: 0031660957     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1021/js980140v     Document Type: Article
Times cited : (112)

References (36)
  • 3
    • 0015502066 scopus 로고
    • The mechanism of autoxidation of myoglobin
    • Misra, H. P.; Fridovich, I. The mechanism of autoxidation of myoglobin. J. Biol. Chem. 1972, 247, 6960-6962.
    • (1972) J. Biol. Chem. , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 4
    • 0001540685 scopus 로고
    • Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin
    • Wever, R.; Oudega, B.; Van Gelder, B. F. Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin. Biochim. Biophys. Acta 1973, 302, 475-478.
    • (1973) Biochim. Biophys. Acta , vol.302 , pp. 475-478
    • Wever, R.1    Oudega, B.2    Van Gelder, B.F.3
  • 5
    • 0018241190 scopus 로고
    • Stability of hemoglobin solution during extended storage
    • De Venuto, F. Stability of hemoglobin solution during extended storage. J. Lab. Clin. Med. 1978, 92, 946-952.
    • (1978) J. Lab. Clin. Med. , vol.92 , pp. 946-952
    • De Venuto, F.1
  • 6
    • 0017209946 scopus 로고
    • Stroma-free haemoglobin solution for infusion: Changes during storage
    • Kramlova, M.; Pristoupil, T. I.; Ulrych, S.; Hrkal, Z. Stroma-free haemoglobin solution for infusion: Changes during storage. Haematologia (Budap.) 1976, 10, 365-371.
    • (1976) Haematologia (Budap.) , vol.10 , pp. 365-371
    • Kramlova, M.1    Pristoupil, T.I.2    Ulrych, S.3    Hrkal, Z.4
  • 7
    • 0026440485 scopus 로고
    • Evaluation of methemoglobin formation during the storage of various hemoglobin solutions
    • Moore, G. L.; Zegna, A.; Ledford, M. E.; Huling J. P.; Fischman, R. M. Evaluation of methemoglobin formation during the storage of various hemoglobin solutions. Artif. Organs 1992, 16, 513-518.
    • (1992) Artif. Organs , vol.16 , pp. 513-518
    • Moore, G.L.1    Zegna, A.2    Ledford, M.E.3    Huling, J.P.4    Fischman, R.M.5
  • 8
    • 0030443567 scopus 로고    scopus 로고
    • Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
    • Chang, B. S.; Kendrick, B. S.; Carpenter, J. F. Surface-induced denaturation of proteins during freezing and its inhibition by surfactants. J Pharm. Sci. 1996, 85, 1325-1330.
    • (1996) J Pharm. Sci. , vol.85 , pp. 1325-1330
    • Chang, B.S.1    Kendrick, B.S.2    Carpenter, J.F.3
  • 9
    • 0023905575 scopus 로고
    • The mechanism of cryoprotection of proteins by solutes
    • Carpenter, J. F.; Crowe, J. H. The mechanism of cryoprotection of proteins by solutes. Cryobiology. 1988, 25, 244-255.
    • (1988) Cryobiology , vol.25 , pp. 244-255
    • Carpenter, J.F.1    Crowe, J.H.2
  • 10
    • 0027272126 scopus 로고
    • Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants
    • Nema, S.; Avis, K. E. Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants. J Parenter. Sci. Technol. 1993, 47, 76-83.
    • (1993) J Parenter. Sci. Technol. , vol.47 , pp. 76-83
    • Nema, S.1    Avis, K.E.2
  • 11
    • 0014356370 scopus 로고
    • Freezing injury in relation to loss of enzyme activities and protection against freezing
    • Heber, U. Freezing injury in relation to loss of enzyme activities and protection against freezing. Cryobiology 1968, 5, 188-201.
    • (1968) Cryobiology , vol.5 , pp. 188-201
    • Heber, U.1
  • 12
    • 0030043206 scopus 로고    scopus 로고
    • Proteins in frozen solutions: Evidence of ice-induced partial unfolding
    • Strambini, G. B.; Gabellieri, E. Proteins in frozen solutions: evidence of ice-induced partial unfolding. Biophys. J. 1996, 70, 971-976.
    • (1996) Biophys. J. , vol.70 , pp. 971-976
    • Strambini, G.B.1    Gabellieri, E.2
  • 13
    • 0028816796 scopus 로고
    • Stability of protein formulations: Investigation of surfactant effects by a novel EPR technique
    • Bam, N. B.; Randolph, T. W.; Cleland, J. L. Stability of protein formulations: investigation of surfactant effects by a novel EPR technique. Pharm. Res. 1995, 12, 2-11.
    • (1995) Pharm. Res. , vol.12 , pp. 2-11
    • Bam, N.B.1    Randolph, T.W.2    Cleland, J.L.3
  • 14
    • 0019316305 scopus 로고
    • Binding of the Triton X series of nonionic surfactants to bovine serum albumin
    • Sukow, W. W.; Sandberg, H. E.; Lewis, E. A.; Eatough, D. J.; Hansen, L. D. Binding of the Triton X series of nonionic surfactants to bovine serum albumin. Biochemistry 1980, 19, 912-917.
    • (1980) Biochemistry , vol.19 , pp. 912-917
    • Sukow, W.W.1    Sandberg, H.E.2    Lewis, E.A.3    Eatough, D.J.4    Hansen, L.D.5
  • 15
    • 0019755006 scopus 로고
    • Characterization of the binding of Triton X-100 to equine and rabbit serum albumin
    • Sukow, W. W.; Bailey, J. Characterization of the binding of Triton X-100 to equine and rabbit serum albumin. Physiol. Chem Phys. 1981, 13, 455-459.
    • (1981) Physiol. Chem Phys. , vol.13 , pp. 455-459
    • Sukow, W.W.1    Bailey, J.2
  • 17
    • 0025892154 scopus 로고
    • The use of surface tension measurements in the design of antibody-based product formulations
    • Levine, H. L.; Ransohoff, T. C.; Kawahata, R. T.; McGregor, W. C. The use of surface tension measurements in the design of antibody-based product formulations. J. Parent. Sci. Technol. 1991, 45, 160-165.
    • (1991) J. Parent. Sci. Technol. , vol.45 , pp. 160-165
    • Levine, H.L.1    Ransohoff, T.C.2    Kawahata, R.T.3    McGregor, W.C.4
  • 18
    • 0020193418 scopus 로고
    • Interaction between hydrophilic proteins and nonionic detergents studied by surface tension measurements
    • Nishikido, N.; Takahara, T.; Kobayashi, H.; Tanaka, M. Interaction between hydrophilic proteins and nonionic detergents studied by surface tension measurements. Bull. Chem. Soc. Jpn. 1982, 55, 3085-3088.
    • (1982) Bull. Chem. Soc. Jpn. , vol.55 , pp. 3085-3088
    • Nishikido, N.1    Takahara, T.2    Kobayashi, H.3    Tanaka, M.4
  • 19
    • 0021244277 scopus 로고
    • Stabilisation of dissolved proteins against denaturation at hydrophobic interfaces
    • Thurow, H.; Geisen, K. Stabilisation of dissolved proteins against denaturation at hydrophobic interfaces. Diabetologia 1984, 27, 212-218.
    • (1984) Diabetologia , vol.27 , pp. 212-218
    • Thurow, H.1    Geisen, K.2
  • 20
    • 0030443488 scopus 로고    scopus 로고
    • Effects of phase separating systems on lyophilized hemoglobin
    • Heller, M. C.; Carpenter, J. F.; Randolph, T. W. Effects of phase separating systems on lyophilized hemoglobin. J. Pharm. Sci. 1996, 85, 1358-1362.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 1358-1362
    • Heller, M.C.1    Carpenter, J.F.2    Randolph, T.W.3
  • 21
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa, T.; Timasheff, S. N. Stabilization of protein structure by sugars. Biochemistry 1982, 21, 6536-6544.
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 22
    • 0028307232 scopus 로고
    • Infrared methods for study of hemoglobin reactions and structures
    • Dong, A.; Caughey, W. S. Infrared methods for study of hemoglobin reactions and structures. Methods Enzymol. 1994, 232, 139-175.
    • (1994) Methods Enzymol. , vol.232 , pp. 139-175
    • Dong, A.1    Caughey, W.S.2
  • 23
    • 0026787050 scopus 로고    scopus 로고
    • Proteins at interfaces: Principles, multivariate aspects, protein resistant surfaces and direct imaging and manipulation of adsorbed proteins
    • Andrade, J. D.; Hlady, V.; Wei, A.-P.; Ho, C.-H.; Lea, A. S.; Jeon, S. I.; Lin, Y. S.; Stroup, E. Proteins at interfaces: Principles, multivariate aspects, protein resistant surfaces and direct imaging and manipulation of adsorbed proteins. Clin. Mater. 1997, 11, 67-84.
    • (1997) Clin. Mater. , vol.11 , pp. 67-84
    • Andrade, J.D.1    Hlady, V.2    Wei, A.-P.3    Ho, C.-H.4    Lea, A.S.5    Jeon, S.I.6    Lin, Y.S.7    Stroup, E.8
  • 25
    • 0006169843 scopus 로고
    • Horbett, T. A., Brash, J. L., Eds.; American Chemical Society: Washington, DC
    • Vogel, V. In Protein at interfaces II: Fundamentals and applications; Horbett, T. A., Brash, J. L., Eds.; American Chemical Society: Washington, DC, 1995; pp 505-518.
    • (1995) Protein at Interfaces II: Fundamentals and Applications , pp. 505-518
    • Vogel, V.1
  • 26
    • 0028925570 scopus 로고
    • Protein destabilization at low temperatures
    • Franks, F. Protein destabilization at low temperatures. Adv. Protein Chem. 1995, 46, 105-139.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 105-139
    • Franks, F.1
  • 27
    • 0028816797 scopus 로고
    • Surface denaturation at solid-void interface - A possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures
    • Hsu, C. C.; Nguyen, H. M.; Yeung, D. A.; Brooks, D. A.; Koe, G. S.; Bewley, T. A.; Pearlman, R. Surface denaturation at solid-void interface - a possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen activator at high temperatures. Pharm. Res. 1995, 12, 69-77.
    • (1995) Pharm. Res. , vol.12 , pp. 69-77
    • Hsu, C.C.1    Nguyen, H.M.2    Yeung, D.A.3    Brooks, D.A.4    Koe, G.S.5    Bewley, T.A.6    Pearlman, R.7
  • 28
    • 0023447349 scopus 로고
    • Conformational changes in proteins induced by low temperatures: An infrared study
    • Casal, H. L.; Kohler, U.; Mantsch, H. H.; Goni, F. M.; Arrondo, J. L. Conformational changes in proteins induced by low temperatures: an infrared study. Z. Naturforsch. 1987, 42, 1339-1342.
    • (1987) Z. Naturforsch. , vol.42 , pp. 1339-1342
    • Casal, H.L.1    Kohler, U.2    Mantsch, H.H.3    Goni, F.M.4    Arrondo, J.L.5
  • 29
    • 0029144157 scopus 로고
    • Role of globin moiety in the autoxidation reaction of oxymyoglobin: Effect of 8 M urea
    • Sugawara, Y.; Matsuoka, A.; Kaino, A.; Shikama, K. Role of globin moiety in the autoxidation reaction of oxymyoglobin: effect of 8 M urea. Biophys. J. 1995, 69, 583-592.
    • (1995) Biophys. J. , vol.69 , pp. 583-592
    • Sugawara, Y.1    Matsuoka, A.2    Kaino, A.3    Shikama, K.4
  • 31
    • 0014691369 scopus 로고
    • Autoxidation of oxymyoglobins
    • Brown, W. D.; Mebine, L. B. Autoxidation of oxymyoglobins. J. Biol. Chem. 1969, 244, 6696-6701.
    • (1969) J. Biol. Chem. , vol.244 , pp. 6696-6701
    • Brown, W.D.1    Mebine, L.B.2
  • 33
    • 0030586740 scopus 로고    scopus 로고
    • Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state
    • Anchordoguy, T. J.; Carpenter, J. F. Polymers protect lactate dehydrogenase during freeze-drying by inhibiting dissociation in the frozen state. Arch. Biochem. Biophys. 1996, 332, 231-238.
    • (1996) Arch. Biochem. Biophys. , vol.332 , pp. 231-238
    • Anchordoguy, T.J.1    Carpenter, J.F.2
  • 34
    • 0026074916 scopus 로고
    • Alkali cation effect on carbonyl-hemoglobin's and -myoglobin's conformer populations when exposed to freeze-concentration of their phosphate-buffered aqueous solutions
    • Astl, G.; Mayer, E. Alkali cation effect on carbonyl-hemoglobin's and -myoglobin's conformer populations when exposed to freeze-concentration of their phosphate-buffered aqueous solutions. Biochim. Biophys. Acta 1991, 1080, 155-159.
    • (1991) Biochim. Biophys. Acta , vol.1080 , pp. 155-159
    • Astl, G.1    Mayer, E.2
  • 35
    • 0017616389 scopus 로고
    • Measurement of the pH of frozen buffer solutions by using pH indicators
    • Orii, Y.; Marita, M. Measurement of the pH of frozen buffer solutions by using pH indicators. J. Biochem. 1977, 81, 163-168.
    • (1977) J. Biochem. , vol.81 , pp. 163-168
    • Orii, Y.1    Marita, M.2
  • 36
    • 0021027685 scopus 로고
    • Structure of human oxyhaemoglobin at 2.1 a resolution
    • Shaanan, B. Structure of human oxyhaemoglobin at 2.1 A resolution. J. Mol. Biol. 1983, 171, 31-59.
    • (1983) J. Mol. Biol. , vol.171 , pp. 31-59
    • Shaanan, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.