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Literature summary extracted from

  • Tomita, S.; Nagasaki, Y.; Shiraki, K.
    Different mechanisms of action of poly(ethylene glycol) and arginine on thermal inactivation of lysozyme and ribonuclease A (2012), Biotechnol. Bioeng., 109, 2543-2552.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
4.6.1.18 Bos taurus
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Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.18 pancreas
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 Bos taurus
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Synonyms

EC Number Synonyms Comment Organism
4.6.1.18 pancreas ribonuclease A
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 Bos taurus
4.6.1.18 ribonuclease A
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 Bos taurus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.6.1.18 additional information
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 L-arginine suppresses heat-induced deamidation and beta-elimination at 98°C, resulting in the suppression of thermal inactivation of bovine pancreas ribonuclease A. Poly(ethylene glycol) with molecular weight 1000 acts as a thermoinactivation suppressor for the protein, especially at higher protein concentrations, while Arg was not effective at higher protein concentrations. Amphiphilic poly(ethylene glycol) and poly(vinylpyrolidone) inhibit intermolecular collision of thermally denatured proteins by preferential interaction with thermally denatured proteins, resulting in the inhibition of intermolecular disulfide exchange, molecular mechanism, overview Bos taurus