经酸、热和去污剂变性的牛红细胞碳酸酐酶B的复性。 - Suppr

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Renaturation of bovine erythrocyte carbonic anhydrase B denatured by acid, heat, and detergent.

作者信息

McCoy L F, Wong K P

出版信息

Biochemistry. 1981 May 26;20(11):3062-7. doi: 10.1021/bi00514a012.

DOI:10.1021/bi00514a012

PMID:6788078

Abstract

摘要

相似文献

Renaturation of bovine erythrocyte carbonic anhydrase B denatured by acid, heat, and detergent.

Biochemistry. 1981 May 26;20(11):3062-7. doi: 10.1021/bi00514a012.

Acid denaturation of bovine carbonic anhydrase B.

Biochemistry. 1974 Jun 18;13(13):2678-83. doi: 10.1021/bi00710a003.

The role of Zn(II) on the folding of bovine carbonic anhydrase B.

Arch Biochem Biophys. 1975 Sep;170(1):12-22. doi: 10.1016/0003-9861(75)90093-4.

The location of tryptophanyl groups in human and bovine carbonic anhydrases. Ultraviolet difference spectra and chemical modification.

Biochim Biophys Acta. 1973 Jan 25;295(1):117-30. doi: 10.1016/0005-2795(73)90079-2.

Role of zinc (II) in the refolding of guanidine hydrochloride denatured bovine carbonic anhydrase.

Biochemistry. 1972 Mar 28;11(7):1314-8. doi: 10.1021/bi00757a031.

Denaturation and reactivation of human carbonic anhydrases in guanidine hydrochloride and urea.

Biochim Biophys Acta. 1973 Jun 15;310(2):376-87. doi: 10.1016/0005-2795(73)90119-0.

Acid denaturation of human carbonic anhydrase B. A fluorimetric kinetic study.

Eur J Biochem. 1974 May 2;44(1):251-9. doi: 10.1111/j.1432-1033.1974.tb03480.x.

Influence of the Zn(II) cofactor on the refolding of bovine carbonic anhydrase after denaturation with sodium dodecyl sulfate.

Anal Chem. 2004 Dec 15;76(24):7151-61. doi: 10.1021/ac0488560.

Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions.

J Biol Chem. 1973 Dec 25;248(24):8518-23.

Studies on the influence of carboxyl-terminal amino acid residues on the activity and stability of human erythrocyte carbonic anhydrase B.

FEBS Lett. 1974 Nov 15;48(2):167-71. doi: 10.1016/0014-5793(74)80459-x.

引用本文的文献

Continuous Fluorescence Depletion Anisotropy Measurement of Protein Rotation.

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Coordination contributions to protein stability in metal-substituted carbonic anhydrase.

J Biol Inorg Chem. 2016 Sep;21(5-6):659-67. doi: 10.1007/s00775-016-1375-6. Epub 2016 Jun 27.

Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.

Biophys J. 2009 Feb 18;96(4):1586-96. doi: 10.1016/j.bpj.2008.11.017.

Solid-phase assisted refolding of carbonic anhydrase using beta-cyclodextrin-polyurethane polymer.

Protein J. 2008 Aug;27(5):334-42. doi: 10.1007/s10930-008-9142-3.

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

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Comparative evaluation of alpha-amylase refolding through two different artificial chaperone systems.

Protein J. 2007 Aug;26(5):293-301. doi: 10.1007/s10930-007-9071-6.

Artificial chaperone-assisted refolding of GuHCl-denatured alpha-amylase at low temperature: refolding versus aggregation.

Protein J. 2005 Jul;24(5):303-13. doi: 10.1007/s10930-005-6751-y.

Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790.

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Renaturation of bovine erythrocyte carbonic anhydrase B denatured by acid, heat, and detergent.

作者信息

McCoy L F, Wong K P

出版信息

Biochemistry. 1981 May 26;20(11):3062-7. doi: 10.1021/bi00514a012.

DOI:10.1021/bi00514a012

PMID:6788078

Abstract

摘要

相似文献

Renaturation of bovine erythrocyte carbonic anhydrase B denatured by acid, heat, and detergent.

Biochemistry. 1981 May 26;20(11):3062-7. doi: 10.1021/bi00514a012.

Acid denaturation of bovine carbonic anhydrase B.

Biochemistry. 1974 Jun 18;13(13):2678-83. doi: 10.1021/bi00710a003.

The role of Zn(II) on the folding of bovine carbonic anhydrase B.

Arch Biochem Biophys. 1975 Sep;170(1):12-22. doi: 10.1016/0003-9861(75)90093-4.

The location of tryptophanyl groups in human and bovine carbonic anhydrases. Ultraviolet difference spectra and chemical modification.

Biochim Biophys Acta. 1973 Jan 25;295(1):117-30. doi: 10.1016/0005-2795(73)90079-2.

Role of zinc (II) in the refolding of guanidine hydrochloride denatured bovine carbonic anhydrase.

Biochemistry. 1972 Mar 28;11(7):1314-8. doi: 10.1021/bi00757a031.

Denaturation and reactivation of human carbonic anhydrases in guanidine hydrochloride and urea.

Biochim Biophys Acta. 1973 Jun 15;310(2):376-87. doi: 10.1016/0005-2795(73)90119-0.

Acid denaturation of human carbonic anhydrase B. A fluorimetric kinetic study.

Eur J Biochem. 1974 May 2;44(1):251-9. doi: 10.1111/j.1432-1033.1974.tb03480.x.

Influence of the Zn(II) cofactor on the refolding of bovine carbonic anhydrase after denaturation with sodium dodecyl sulfate.

Anal Chem. 2004 Dec 15;76(24):7151-61. doi: 10.1021/ac0488560.

Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions.

J Biol Chem. 1973 Dec 25;248(24):8518-23.

Studies on the influence of carboxyl-terminal amino acid residues on the activity and stability of human erythrocyte carbonic anhydrase B.

FEBS Lett. 1974 Nov 15;48(2):167-71. doi: 10.1016/0014-5793(74)80459-x.

引用本文的文献

Continuous Fluorescence Depletion Anisotropy Measurement of Protein Rotation.

J Fluoresc. 2018 Mar;28(2):533-542. doi: 10.1007/s10895-018-2214-7. Epub 2018 Feb 3.

Coordination contributions to protein stability in metal-substituted carbonic anhydrase.

J Biol Inorg Chem. 2016 Sep;21(5-6):659-67. doi: 10.1007/s00775-016-1375-6. Epub 2016 Jun 27.

Exploring local flexibility/rigidity in psychrophilic and mesophilic carbonic anhydrases.

Biophys J. 2009 Feb 18;96(4):1586-96. doi: 10.1016/j.bpj.2008.11.017.

Solid-phase assisted refolding of carbonic anhydrase using beta-cyclodextrin-polyurethane polymer.

Protein J. 2008 Aug;27(5):334-42. doi: 10.1007/s10930-008-9142-3.

Carbonic anhydrase as a model for biophysical and physical-organic studies of proteins and protein-ligand binding.

Chem Rev. 2008 Mar;108(3):946-1051. doi: 10.1021/cr050262p.

Comparative evaluation of alpha-amylase refolding through two different artificial chaperone systems.

Protein J. 2007 Aug;26(5):293-301. doi: 10.1007/s10930-007-9071-6.

Artificial chaperone-assisted refolding of GuHCl-denatured alpha-amylase at low temperature: refolding versus aggregation.

Protein J. 2005 Jul;24(5):303-13. doi: 10.1007/s10930-005-6751-y.

Extracellular and cellular distribution of muramidase-2 and muramidase-1 of Enterococcus hirae ATCC 9790.

J Bacteriol. 1992 May;174(10):3236-41. doi: 10.1128/jb.174.10.3236-3241.1992.