메뉴 건너뛰기




Volumn 59, Issue 3, 1998, Pages 281-285

II. Electrostatic effect in the aggregation of heat-denatured RNase A and implications for protein additive design

Author keywords

Protein additives; Protein aggregation; Protein formulation; RNase A

Indexed keywords

ADDITIVES; ELECTROSTATICS; ENZYMES; MIXING; MOLECULAR ORIENTATION; MOLECULES; PH; POLYMERS; SODIUM COMPOUNDS;

EID: 0032486768     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980805)59:3<281::AID-BIT3>3.0.CO;2-7     Document Type: Article
Times cited : (42)

References (15)
  • 1
    • 0027976442 scopus 로고
    • Dextran-coated superparamagnetic iron oxides, an MR contrast agent for assessing lymph nodes in the head and neck
    • Anzai, Y., Mclachlan, S., Morris, M., Saxton, R., Lufkin, R. B. 1994. Dextran-coated superparamagnetic iron oxides, an MR contrast agent for assessing lymph nodes in the head and neck. Am. J. Neuroradiol. 15: 87-94.
    • (1994) Am. J. Neuroradiol. , vol.15 , pp. 87-94
    • Anzai, Y.1    Mclachlan, S.2    Morris, M.3    Saxton, R.4    Lufkin, R.B.5
  • 2
    • 0031581052 scopus 로고    scopus 로고
    • Inhibition of human breast epithelial HBL100 cell proliferation by a dextran derivative (CMDB7) with the FGF2 autocrine loop
    • Bagheri-Yarmand, R., Liu, J. F., Ledoux, D., Morere, J. F., Crepin, M. 1997. Inhibition of human breast epithelial HBL100 cell proliferation by a dextran derivative (CMDB7) with the FGF2 autocrine loop. Biochem. Biophys. Res. Commun. 239: 424-428.
    • (1997) Biochem. Biophys. Res. Commun. , vol.239 , pp. 424-428
    • Bagheri-Yarmand, R.1    Liu, J.F.2    Ledoux, D.3    Morere, J.F.4    Crepin, M.5
  • 4
    • 0028111599 scopus 로고
    • Properties of a recombinant human hemoglobin double mutant: Sickle hemoglobin with Leu-88(β) at the primary aggregation site substituted by Ala
    • De Llano, J. J. M., Manning, J. M. 1994. Properties of a recombinant human hemoglobin double mutant: sickle hemoglobin with Leu-88(β) at the primary aggregation site substituted by Ala. Prot. Sci. 3: 1206-1212.
    • (1994) Prot. Sci. , vol.3 , pp. 1206-1212
    • De Llano, J.J.M.1    Manning, J.M.2
  • 5
    • 0022609463 scopus 로고
    • The design and synthesis of detergents for membrane biochemistry
    • Hjelmeland, L. M. 1986. The design and synthesis of detergents for membrane biochemistry. Meth. Enzymol. 124: 135-164.
    • (1986) Meth. Enzymol. , vol.124 , pp. 135-164
    • Hjelmeland, L.M.1
  • 6
    • 0018905501 scopus 로고
    • Dilute iron dextran formulation for addition to parenteral nutrient solutions
    • Kwong, K. W., Tsallas, G. 1980. Dilute iron dextran formulation for addition to parenteral nutrient solutions. Am. J Hosp. Pharm. 37: 206-210.
    • (1980) Am. J Hosp. Pharm. , vol.37 , pp. 206-210
    • Kwong, K.W.1    Tsallas, G.2
  • 7
    • 0029637153 scopus 로고
    • Approaches for increasing the solution stability of proteins
    • Manning, M. C., et al. 1995. Approaches for increasing the solution stability of proteins. Biotechnol. Bioeng. 48: 506-512.
    • (1995) Biotechnol. Bioeng. , vol.48 , pp. 506-512
    • Manning, M.C.1
  • 8
    • 0029973872 scopus 로고    scopus 로고
    • Extracorporeal removal of lipids by dextran sulfate cellulose adsorption
    • Olbricht, C. J. 1996. Extracorporeal removal of lipids by dextran sulfate cellulose adsorption. Artif. Organs 20: 332-335.
    • (1996) Artif. Organs , vol.20 , pp. 332-335
    • Olbricht, C.J.1
  • 9
    • 0029559003 scopus 로고
    • Stability and stabilization of insulinotropin in a dextran formulation
    • Qi, H., Heller, D. L. 1995. Stability and stabilization of insulinotropin in a dextran formulation. PDA J. Pharm. Sci. Technol. 49: 289-293.
    • (1995) PDA J. Pharm. Sci. Technol. , vol.49 , pp. 289-293
    • Qi, H.1    Heller, D.L.2
  • 10
    • 0014940381 scopus 로고
    • The gross conformation of protein-sodium dodecyl sulfate complexes
    • Reynolds, J. A., Tanford, J. 1970. The gross conformation of protein-sodium dodecyl sulfate complexes. J. Biol. Chem. 245: 5161-5165.
    • (1970) J. Biol. Chem. , vol.245 , pp. 5161-5165
    • Reynolds, J.A.1    Tanford, J.2
  • 11
    • 0016506214 scopus 로고
    • Binding isotherms of sodium dodecyl sulfate to protein polypeptides with special reference to SDS-polyacrylamide gel electrophoresis
    • Takagi, T., Tsuji, K., Shirahama, K. 1975. Binding isotherms of sodium dodecyl sulfate to protein polypeptides with special reference to SDS-polyacrylamide gel electrophoresis. J. Biochem. 77: 939-947.
    • (1975) J. Biochem. , vol.77 , pp. 939-947
    • Takagi, T.1    Tsuji, K.2    Shirahama, K.3
  • 12
    • 0345455600 scopus 로고
    • Hydrogen ion equilibria of ribonuclease
    • Tanford, C., Hauenstein, J. D. 1956. Hydrogen ion equilibria of ribonuclease. J. Am. Chem. Soc. 78: 5287-5291.
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 5287-5291
    • Tanford, C.1    Hauenstein, J.D.2
  • 14
    • 0032486770 scopus 로고    scopus 로고
    • The study of protein aggregation due to heat denaturation: A structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering
    • 000-000
    • Tsai, A.M., van Zanten, J. H., Betenbaugh, M.J. 1998. The study of protein aggregation due to heat denaturation: a structural approach using circular dichroism spectroscopy, nuclear magnetic resonance, and static light scattering. Biotechnol. Bioeng. 59: 000-000.
    • (1998) Biotechnol. Bioeng. , vol.59
    • Tsai, A.M.1    Van Zanten, J.H.2    Betenbaugh, M.J.3
  • 15
    • 0030929864 scopus 로고    scopus 로고
    • Dependence of the molecular mobility and protein stability of freeze-dried gamma-globulin formulations on the molecular weight of dextran
    • Yoshioka, S., Aso, Y., Kojuma, S. 1997. Dependence of the molecular mobility and protein stability of freeze-dried gamma-globulin formulations on the molecular weight of dextran. Pharm. Res. 14: 736-741.
    • (1997) Pharm. Res. , vol.14 , pp. 736-741
    • Yoshioka, S.1    Aso, Y.2    Kojuma, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.