Adsorption properties of hemoglobin

Atyaksheva, L. F.; Dobryakova, I. V.; Ivanova, I. I.; Knyazeva, E. E.; Ovsyannikov, R. A.; Chukhrai, E. S.

doi:10.1134/s0036024412030041

Cited by 10 publications

(1 citation statement)

References 15 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One such model protein is bovine haemoglobin (bHb), which is economical, easily available, well-characterised, and has been used in numerous studies [3] , [4] , [5] . Hb is an oxygen-carrying transport protein with a molecular weight of 64.5 kDa and a diameter of approximately 5 nm [6] , [7] . It exists as a tetramer comprising two α- and two β-globin chains which are bound to each other by hydrogen bonding, salt bridges and hydrophobic interactions.…”

Section: Introductionmentioning

confidence: 99%

The thermal and storage stability of bovine haemoglobin by ultraviolet–visible and circular dichroism spectroscopies

Bhomia

Trivedi

Coleman

et al. 2016

Journal of Pharmaceutical Analysis

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 99%

The thermal and storage stability of bovine haemoglobin by ultraviolet–visible and circular dichroism spectroscopies

Bhomia

Trivedi

Coleman

et al. 2016

Journal of Pharmaceutical Analysis

View full text Add to dashboard Cite

show abstract

Interparticle mesoporous silica as an effective support for enzyme immobilisation

et al. 2014

View full text Add to dashboard Cite

Mesoporous silica materials with cylindrical pores (MPSC) and interparticle pore structures (IPMPS) were synthesized by typical sol-gel methods, and their structural properties were characterized. The enzyme immobilised on IPMPS exhibited higher specific reactivity because of an improvement in the substrate affinity of the enzyme immobilised on the pore spaces of the IPMPS support. Fourier transform infrared and circular dichroism spectroscopy indicated that the highly ordered structure of formaldehyde dehydrogenase (FDH) is not altered by binding to IPMPS and MPSC surfaces. Interestingly, after 10 repeated reactions, FDH immobilised on IPMPS exhibited a residual activity higher than that of FDH immobilised on MPSC. The cycle performance of the enzyme immobilised on MPSC decreased because of support aggregation by the released enzyme. Meanwhile, IPMPS has a high-intensity surface electrical charge that is highly dispersible in the presence of enzymes. In addition, enzymes that were inactive because of being buried inside mesopores are quantitatively determined. The dependency of the activity of FDH immobilised on IPMPS and MPSC as a function of substrate (formaldehyde) concentration was also evaluated to determine the potential application of these materials as biosensors. Formaldehyde concentrations of 3.0-500 mM could be detected using FDH immobilised on the IPMPS support.

show abstract