ArticleJournal of pharmaceutical analysis2016
The thermal and storage stability of bovine haemoglobin by ultraviolet-visible and circular dichroism spectroscopies.
Article in Journal of pharmaceutical analysis, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Precise Engineering and Efficient Biosynthesis of Robust and High-Activity Human Haemoglobin for Artificial Oxygen Carriers.Microbial biotechnology · 2025Article
- Interactions Between Silver Nanoparticles and Culture Medium Biomolecules with Dose and Time Dependencies.Journal of fluorescence · 2025Article
- Characteristics of a Spray-Dried Porcine Blood Meal forInsects · 2024Article
- Interfacial Denaturation at the Droplet Simplifies the Formation of Drug-Loaded Protein Nanocapsules to Enhance Immune Response of Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Article
- Expanding the reactivity of inorganic clusters towards proteins: the interplay between the redox and hydrolytic activity of Ce(iv)-substituted polyoxometalates as artificial proteases.Chemical science · 2021Article
- Myristic Acid Coated Protein Immobilised Mesoporous Silica Particles as pH Induced Oral Delivery System for the Delivery of Biomolecules.Pharmaceuticals (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The effects of temperature, pH and long-term storage on the secondary structure and conformation changes of bovine haemoglobin (bHb) were studied using circular dichroism (CD) and ultraviolet--visible (UV-vis) spectroscopies. Neural network software was used to deconvolute the CD data to obtain the fractional content of the five secondary structures. The storage stability of bHb solutions in pH 6, 7 and 8 buffers was significantly higher at 4 °C than at 23 °C for the first 3 days. A complete denaturation of bHb was observed after 40 days irrespective of storage temperature or pH. The bHb solutions were also exposed to heating and cooling cycles between 25 and 65 °C and structural changes were followed by UV-vis and CD spectroscopies. These experiments demonstrated that α-helix content of bHb decreased steadily with the increasing temperature above 35 °C at all pH values. The loss in α-helicity and gain in random coil conformations was pH-dependent and the greatest under alkaline conditions. Furthermore, there was minimal recovery of the secondary structure content upon cooling to 25 °C. The use of bHb as a model drug is very common and this study elucidates the significance of storage and processing conditions on its stability.
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