Separation of two forms of glutathione peroxidase from human erythrocytes by hydrophobic chromatography
- 1 January 1985
- journal article
- research article
- Published by Elsevier in Journal of Chromatography A
- Vol. 330 (2) , 383-387
- https://doi.org/10.1016/s0021-9673(01)81999-3
Abstract
No abstract availableThis publication has 9 references indexed in Scilit:
- Protein hydrophobicity and stability support the thermodynamic theory of protein degradationBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
- Mechanism of Protein Hydrophobic Chromatography. Protein Unfolding and its Contribution to Effective HydrophobicityPreparative Biochemistry, 1984
- Separation of hydrophobic and hydrophilic forms of γ-glutamyltransferase from human serum by hydrophobic chromatography on phenyl-Sepharose CL-4B: studies on normal sera and sera of patients with liver diseaseClinica Chimica Acta; International Journal of Clinical Chemistry, 1984
- [44] Glutathione peroxidasePublished by Elsevier ,1981
- Selenium-Dependent EnzymesAnnual Review of Biochemistry, 1980
- Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic seriesArchives of Biochemistry and Biophysics, 1977
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Purification and properties of human erythrocyte glutathione peroxidase.Journal of Biological Chemistry, 1975
- Glutathione Peroxidase: The Primary Agent for the Elimination of Hydrogen Peroxide in Erythrocytes*Biochemistry, 1963