Papers by Keyword: Myoglobin

Abstract: The knowledge on human tissue is very important to recognize desirable properties of biomaterials. Host cells, extracellular matrix, integrated vessels and interstitial fluids create a complex and dynamic system able to regenerate and respond to environmental stimuli. Myoglobin is a protein with most of α-helices on its secondary structure, and responsible for oxygen binding and release in muscles, by the heme group. This work investigates the Mb adsorption process onto zinc-hydroxyapatite (ZnHA) surface by spectroscopic studies. To do so, ZnHA (0.05 g) was incubated with 4mL of 2mg Mb/mL on phosphate buffer solution pH 6.0 for 24h at 37°C. The FTIR analyses of ZnHA powders before and after protein adsorption provided information concerning the protein content. UV-Vis spectrocopy in the reflectance mode suggested a mixture of MbO₂ and Met Mb on lyophilized solid Mb, and the prevalence of MetMb form when Mb was adsorbed on ZnHA sample. The decrease of UV-Vis secondary bands suggests interactions through the Mb heme group and the ZnHA surfaces. Circular Dichroism (CD) spectroscopy indicated the maintenance of the Mb α-helices secondary structure after the adsorption process on ZnHA powders.

Abstract: Ammonium sulfate fractionation was implicated as one of essential steps to purified Myoglobin (Mb).We adopted SDS-PAGE analysis and absorption spectra scanning to demonstrate the effect of ammonium sulfate on Mb and its derivatives. The results shown that protein with the molecular weight above 37.8kDa were dominated in myoglobin extract of tilapia, which can be precipitated with ammonium sulfate. Mb molecular weight of tilapia is about 15.8 kDa, which can be collected by the treatment of ammonium sulfate with saturation between 60%-70% to remove unwanted protein. The absorption spectra show that Mb derivatives could be transferred to met-myoglobin after preliminary fractionating with ammonium sulfate.

Abstract: In this work myoglobin (Mb) adsorption was carried out in a batch system using hydroxyapatite (HA) powder during 24 hours at 37°C. The HA samples were analyzed after protein adsorption by Fourier Transformed Infrared (FTIR) and UV-Vis Spectroscopy in reflectance mode. UV-Vis analyses showed that Soret and Q bands shifted to lower wavelengths when Mb is associated with HA surface. This result suggests that Mb Heme group is sensitive to the protein adsorption onto HA surface. HA disks coated with myoglobin and cultured with human osteoblastic cells during 7 days showed that cell adhesion and proliferation were not inhibited by the protein coating after 7 days in cell culture.