Volume effects produced by protein-ion interactions. The binding of bovine plasma albumin with thiocyanate and trichloroacetate ions.
作者信息
Katz S, Crissman J K, Roberson L C
出版信息
J Biol Chem. 1974 Dec 25;249(24):7892-5.
PMID:4473452
Abstract
摘要
相似文献
1
Volume effects produced by protein-ion interactions. The binding of bovine plasma albumin with thiocyanate and trichloroacetate ions.
J Biol Chem. 1974 Dec 25;249(24):7892-5.
2
Effects of salts and pH on the binding of thiocyanate with bovine plasma albumin.
J Biol Chem. 1968 May 10;243(9):2328-36.
3
The adsorption of some proteins on hydroxylapatite and other absorbents used for chromatographic separations.
Biochim Biophys Acta. 1974 May 10;351(1):57-76. doi: 10.1016/0005-2795(74)90065-8.
4
Chemical relaxation studies on bovine serum albumin.
FEBS Lett. 1974 Apr 15;41(1):43-5. doi: 10.1016/0014-5793(74)80949-x.
5
Trapping of benzo(a)pyrene by bovine serum albumin.
Biochim Biophys Acta. 1974 Sep 13;365(1):181-92. doi: 10.1016/0005-2795(74)90262-1.
6
Chemical relaxation studies on bovine serum albumin. I. Reactions of the imidazole groups at pH 6 to 8.
Biophys Chem. 1974 Apr;1(4):300-7. doi: 10.1016/0301-4622(74)80016-5.
7
8
Gibbs-Donnan and adsorption effects in the study of the binding of Fminus to albumin by gel filtration.凝胶过滤法研究氟离子与白蛋白结合中的吉布斯-唐南效应和吸附效应
Biochim Biophys Acta. 1974 Apr 11;342(2):333-42. doi: 10.1016/0005-2795(74)90088-9.
9
pK change of imidazole groups in bovine serum albumin due to the conformational change at neutral pH.在中性pH条件下，牛血清白蛋白中咪唑基团因构象变化而导致的pK变化。
Biochemistry. 1971 Aug 17;10(17):3217-21. doi: 10.1021/bi00793a009.
10
The kinetics of dissociation of Cu2+-bovine serum albumin biuret complexes.
J Biol Chem. 1973 Sep 10;248(17):6129-34.
引用本文的文献
1
Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite.线粒体三磷酸腺苷酶的动力学机制。叠氮化物的抑制作用和亚硫酸盐的激活作用。
Biochem J. 1982 Jan 15;202(1):15-23. doi: 10.1042/bj2020015.
Zotero 插件