2016
DOI: 10.1080/09168451.2016.1189317
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Development of a simple assay system for protein-stabilizing efficiency based on hemoglobin protection against denaturation and measurement of the cooperative effect of mixing protein stabilizers

Abstract: We have elucidated the cooperative stabilization of proteins by sugars, amino acids, and other protein-stabilizing agents using a new and simple assay system. Our system determines the protein-stabilizing ability of various compounds by measuring their ability to protect hemoglobin from denaturation. Hemoglobin denaturation was readily measured by quantitative changes in its ultraviolet-visible absorption spectrum. The efficiency of our assay was confirmed using various sugars such as trehalose and sucrose tha… Show more

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Cited by 9 publications
(6 citation statements)
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“…Glycine and proline showed a certain ability to stabilize hemoglobin [68]. It was proposed that proline with a concentration of >3 M behaves as an enzyme stabilizer as well as a protein solubilizing solute and forms an amphipathic supramolecular assembly and successfully thwarts the aggregation associated with the refolding of bovine carbonic anhydrase [43].…”
Section: Purification Of Animal Proteins By Membrane Techniquesmentioning
confidence: 99%
“…Glycine and proline showed a certain ability to stabilize hemoglobin [68]. It was proposed that proline with a concentration of >3 M behaves as an enzyme stabilizer as well as a protein solubilizing solute and forms an amphipathic supramolecular assembly and successfully thwarts the aggregation associated with the refolding of bovine carbonic anhydrase [43].…”
Section: Purification Of Animal Proteins By Membrane Techniquesmentioning
confidence: 99%
“…Compared with MC 0.1% and MC 0.5%, which retained residual FGF-2 contents of 36.9% and 13.4%, respectively, after 2 h at 37 °C, MC 0.05% could retain 81% of baseline FGF-2 content after similar heat exposure. As no single excipient was able to sufficiently stabilise FGF-2 against thermal degradation at 37 °C, combinations of the excipients were applied to evaluate for synergistic effects [31][32][33]. Combinations of MC 0.05% w/v with either alanine 20 mM, HSA 1 mg/mL or both alanine 20 mM and HSA 1 mg/mL, were evaluated.…”
Section: Stabilisation Of Fgf-2 Solutions To Temperature Stressorsmentioning
confidence: 99%
“…To facilitate discussion, the blank vehicles and corresponding FGF-2 formulations will henceforth be identified by their respective ID as listed in Table 3. As no single excipient was able to sufficiently stabilise FGF-2 against thermal degradation at 37 • C, combinations of the excipients were applied to evaluate for synergistic effects [31][32][33]. Combinations of MC 0.05% w/v with either alanine 20 mM, HSA 1 mg/mL or both alanine 20 mM and HSA 1 mg/mL, were evaluated.…”
Section: Stabilisation Of Fgf-2 Solutions To Temperature Stressorsmentioning
confidence: 99%
“…This is particularly relevant for some proteins, such as Hb, that display a strong structure-function relationship. Thus, protein stabilizers have emerged as a powerful strategy to increase their shelf life during both storage and delivery [24,29]. Amongst them, TRE, which is a naturally occurring osmolyte and an often used pharmaceutical excipient, is regarded as an excellent stabilizer, due to its ability to preserve proteins' functionality both in solution and as freeze-dried products [30].…”
Section: Hb Stabilization With Trementioning
confidence: 99%