Inhibition of Ribonuclease Activity by Bentonite
| Autor: | L. Lavkulich, W. P. Ronald, G. G. Jacoli |
|---|---|
| Rok vydání: | 1973 |
| Předmět: |
Protein Denaturation
Potassium chemistry.chemical_element complex mixtures Ribonucleases Adsorption X-Ray Diffraction Cation-exchange capacity Ribonuclease Edetic Acid chemistry.chemical_classification Analysis of Variance biology Computers Oxides Barium General Medicine Hydrogen-Ion Concentration Enzyme assay Ion Exchange Enzyme chemistry Biochemistry Bentonite biology.protein Aluminum Silicates Nuclear chemistry |
| Zdroj: | Canadian Journal of Biochemistry. 51:1558-1565 |
| ISSN: | 0008-4018 |
| DOI: | 10.1139/o73-210 |
| Popis: | The inhibition of ribonuclease activity by bentonite and the adsorption of the protein molecule within the clay matrix were assessed by enzyme and X-ray diffraction analysis, respectively.Pretreatment of bentonite with EDTA, potassium, barium, and barium–EDTA caused varying expansion of the d(001) spacing of the clay. The d(001) variation was sensitive to pH.Inhibition of the enzyme activity generally followed the pattern of expansion of the d(001) spacing of the clay, but failed when the interlayers of bentonite expanded beyond their maximum capability.Vermiculite, which is a clay having a higher cation exchange capacity than bentonite, did not expand from the normal state after similar treatment nor did it inhibit ribonuclease activity.When the secondary and tertiary structures of the protein molecule were disrupted, the denatured protein still entered the interlayers of bentonite, but caused a greater expansion of the d(001) spacing than the native ribonuclease. |
| Databáze: | OpenAIRE |
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