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A hybrid PHB-hydroxyapatite composite for biomedical application: Production, in vitro and in vivo investigation / E. I. Shishatskaya, I. A. Khlusov, T. G. Volova // Journal of Biomaterials Science, Polymer Edition. - 2006. - Vol. 17, Is. 5. - P481-498, DOI 10.1163/156856206776986242 . - ISSN 0920-5063
Кл.слова (ненормированные):
Biocompatibility -- Hydroxyapatite (HA) -- PHB-hydroxyapatite composite -- Polyhydroxyalkanoate (PHA) -- Polyhydroxybutyrate (P(3HB)) -- Properties -- Biocompatibility -- Differential thermal analysis -- Electron microscopy -- Free energy -- Interfacial energy -- Physical properties -- Surface properties -- X ray analysis -- Biomedical application -- Physicochemical properties -- Polyhydroxyalkanoate (PHA) -- Polyhydroxybutyrate (PHB) -- Hydroxyapatite -- hydroxyapatite -- poly(3 hydroxybutyric acid) -- polymer -- biomaterial -- hydroxybutyric acid -- adhesion -- animal cell -- animal tissue -- article -- biomedicine -- bone marrow cell -- cell differentiation -- cell growth -- chemical structure -- composite material -- controlled study -- crystallization -- decomposition -- electron microscopy -- in vitro study -- in vivo study -- melting point -- mouse -- nonhuman -- ossification -- osteoblast -- physical chemistry -- priority journal -- rat -- strength -- structure analysis -- surface property -- synthesis -- temperature measurement -- thermal analysis -- tissue engineering -- wettability -- animal -- biomechanics -- bioremediation -- bone prosthesis -- cattle -- cell culture -- chemistry -- cytology -- differential scanning calorimetry -- drug effect -- human -- materials testing -- prostheses and orthoses -- scanning electron microscopy -- standard -- Wistar rat -- Murinae -- Animals -- Biocompatible Materials -- Biodegradation, Environmental -- Biomechanics -- Bone Substitutes -- Cattle -- Cells, Cultured -- Differential Thermal Analysis -- Durapatite -- Humans -- Hydroxybutyrates -- Materials Testing -- Microscopy, Electron, Scanning -- Osteoblasts -- Prostheses and Implants -- Rats -- Rats, Wistar -- Surface Properties
Аннотация: Samples of a hybrid composite of polyhydroxybutyrate (PHB), a biodegradable polyester, and hydroxyapatite (HA), with different PHB/HA ratios, have been prepared using mechanical-physical method. Electron microscopy, X-ray structure analysis and differential thermal analysis have been used to investigate the structure and physicochemical properties of the composite, depending on the PHB/HA ratio. The properties of the surface of the HA-loaded composite are significantly different from those of the pure polymer. As the HA percentage in the composite increases, free interface energy, the cohesive force, i.e., the strength of the adhesive bond between the composite surface and the water phase, and surface wettability increase. The HA percentage of the composite does not influence its melting temperature, but affects the temperature for the onset of decomposition: as the HA content increases from 0 to 10% (w/w), Td decreases from 260В°C to 225В°C. The degree of crystallinity of PHB/HA increases from 77% to 89% with an increase in the HA fraction from 10% to 50%. Functional properties of the composites have been investigated in vitro and in vivo. The best parameters of growth and differentiation of murine marrow osteoblasts are registered on PHB/HA samples containing 10% and 20% HA. In ectopic bone formation assay it has been proven that the hybrid PHB/HA composites can function as scaffolds and that bone tissue develops on their surface and in pores. В© VSP 2006.

Scopus
Держатели документа:
Institute of Biophysics, Siberian Branch, Russian Academy of Sciences, Akademgorodok, Krasnoyarsk 60036, Russian Federation
Tomsk State University, Tomsk 634021, Russian Federation : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Shishatskaya, E.I.; Khlusov, I.A.; Volova, T.G.

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Purification and characterization of flavoproteins and cytochromes from the yellow bioluminescence marine bacterium Vibrio fischeri strain Y1 / V. N. Petushkov, J. Lee // European Journal of Biochemistry. - 1997. - Vol. 245, Is. 3. - P790-796 . - ISSN 0014-2956
Кл.слова (ненормированные):
anisotropy -- lumazine protein -- Photobacterium -- thioredoxin reductase -- time-resolved fluorescence -- cytochrome -- flavoprotein -- article -- bioluminescence -- nonhuman -- priority journal -- protein analysis -- protein purification -- sea -- vibrio -- Amino Acid Sequence -- Bacterial Proteins -- Cytochromes -- Flavoproteins -- Molecular Sequence Data -- Sequence Alignment -- Vibrio -- Azotobacter -- Bacteria (microorganisms) -- Escherichia coli -- Haemophilus -- haemophilus influenza -- Murinae -- Negibacteria -- Photobacterium -- Photobacterium leiognathi -- Pseudomonas -- uncultured marine bacterium -- Vibrio fischeri
Аннотация: Several flavoproteins and cytochromes that occur as major components in extracts of the yellow bioluminescence Y1 strain of the murine bacterium Vibrio fischeri have been purified and characterized with respect to their mass (SDS/PAGE) and matrix-assisted laser-desorption/ionization MS), chromatographic properties, N-terminal sequence, and spectroscopy (absorption, fluorescence emission and anisotropy decay). The investigated proteins were as follows: yellow fluorescence protein (YFP) with bound riboflavin, FMN or 6,7-dimethyl-8-ribityllumazine; a blue fluorescence protein (BFP) with bound 6,7-dimethyl-8-ribityllumazine, riboflavin, or 6- methyl-7-oxo-ribityllumazine; thioredoxin reductase with FAD as ligand; and two c-type diheme cytochromes, c551 and c554. We present evidence that the riboflavin-bound YFP has an N-terminal sequence corresponding to that published for the dimeric YFP. We show that an equilibrium replacement of the riboflavin can be made with excess lumazine derivative and that lumazine- bound YFP has different bioluminescence properties to those of the lumazine protein from Photobacterium leiognathi. BFP is a different protein again, and in the bacterial lysate it occurs in multiple forms, ligated to either riboflavin, lumazine, or t he 7-oxolumazine derivative. The N-terminal sequence for BFP-shows similarities to those of the YFP proteins and to lumazine protein and riboflavin synthase from Photobacterium. BFP in any form has no bioluminescence or riboflavin-synthase activity. A 70-kDa fluorescent flavoprotein with FAD as ligand has an N-terminal sequence highly similar to those of thioredoxin reductases from Haemophilus influenza and Escherichia coli. Cytochrome contaminations in previous preparations of YFP have been removed and an identified as the two c-type cytochromes c551 and c554. Both inhibit the NADH-induced bioluminescence in the reductase/luciferase system with the luciferase from P. leiognathi and V. fischeri. The N-terminal amino acid sequence of the cytochrome (c551) corresponds to a diheme cytochrome c4. The spectral properties of c554 are similar to those of other c5 cytochromes, and both c554 and c551 have absorption spectra similar to those of the respective cytochromes from the gram-negative bacteria Pseudomonas and Azotobacter.

Scopus
Держатели документа:
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA, United States
Institute of Biophysics, Academy of Sciences of Russia, Krasnoyarsk, Russian Federation
Dept. of Biochem. and Molec. Biology, University of Georgia, Athens, GA 30602, United States : 660036, Красноярск, Академгородок, д. 50, стр. 50

Доп.точки доступа:
Petushkov, V.N.; Lee, J.

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