The effects of allantoin, arginine and NaCl on thermal melting and aggregation of ribonuclease, bovine serum albumin and lysozyme
| Autor: | Tsutomu Arakawa, Nasib Karl Maluf |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Isothermal microcalorimetry Protein Denaturation 030103 biophysics Circular dichroism Arginine 02 engineering and technology Sodium Chloride Biochemistry Protein Aggregates 03 medical and health sciences chemistry.chemical_compound Ribonucleases Allantoin Structural Biology Animals Ribonuclease Solubility Bovine serum albumin Molecular Biology Chromatography biology Temperature Proteins Serum Albumin Bovine General Medicine 021001 nanoscience & nanotechnology chemistry biology.protein Cattle Muramidase Lysozyme 0210 nano-technology |
| Zdroj: | International Journal of Biological Macromolecules. 107:1692-1696 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2017.10.034 |
| Popis: | Allantoin is widely used as a skin care agent and readily forms crystals, which were recently shown to bind endotoxins and high molecular weight aggregates in cell culture harvests. Here, we have investigated the effects of allantoin on thermal stability and aggregation of protein using ribonuclease, bovine serum albumin and lysozyme using temperature-regulated circular dichroism (CD) and differential scanning microcalorimetry (DSC). Ribonuclease showed no change in thermal stability and aggregation by the addition of allantoin. While allantoin showed no effects on the thermal stability of bovine serum albumin, it enhanced aggregation. Similarly, allantoin showed no stabilizing effects on lysozyme, but it strongly suppressed aggregation. Such suppressed aggregation resulted in reversibility of thermal unfolding of lysozyme. These effects of allantoin were then compared with those of NaCl and arginine hydrochloride. Arginine was similar to allantoin at low concentrations, where both solvent additives can be compared due to limited solubility of allantoin. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect