Human erythrocyte catalase: An improved method of isolation and a reevaluation of reported properties
Autor: | Joseph Bonaventura, Suen Fang, Walter A. Schroeder |
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Rok vydání: | 1972 |
Předmět: |
Erythrocytes
Ultraviolet Rays Biophysics chemistry.chemical_element Hemolysis Biochemistry Oxygen Chromatography DEAE-Cellulose chemistry.chemical_compound Spectrophotometry medicine Chemical Precipitation Humans Amino Acids Cellulose Molecular Biology Heme chemistry.chemical_classification Carbon Monoxide Chromatography biology medicine.diagnostic_test Lability Catalase Chromatography Ion Exchange medicine.disease Amino acid chemistry Ammonium Sulfate Yield (chemistry) biology.protein Ion Exchange Resins Mathematics |
Zdroj: | Archives of Biochemistry and Biophysics. 150:606-617 |
ISSN: | 0003-9861 |
Popis: | An improved method for the isolation of human erythrocyte catalase from large volumes of cells is described. Time of isolation has been reduced and the need for larger equipment has been minimized. The yield is 200–300 mg per liter of packed cells. Amino acid composition, molecular weight, spectral constants, heme content, activity, and N-terminal residues have been determined. Although the isolative procedure is a modification of that of Morikofer-Zwez et al. (1969) (Eur. J. Biochem.11:49), the lability of the product toward oxygen as reported by them has not been observed nor has it been possible to produce extensive changes in properties of the material by subjecting it to the adverse conditions that they describe. However, by chromatographic procedures, it has been shown that the catalase immediately after isolation has a heterogeneity different than they describe and that alteration with time does occur. The cause of the heterogeneity has not been determined. |
Databáze: | OpenAIRE |
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