



@article {2447,
	title = {Biological evaluation of calcium alginate microspheres as a vehicle for the localized delivery of a therapeutic enzyme},
	journal = {Journal of Biomedical Materials Research - Part AJ. Biomed. Mater. Res. Part A},
	volume = {74},
	year = {2005},
	note = {Cited By (since 1996): 12Export Date: 21 November 2012Source: ScopusCODEN: JBMRCdoi: 10.1002/jbm.a.30348PubMed ID: 16028235Language of Original Document: EnglishCorrespondence Address: Barrias, C.C.; Instituto de Engenharia Biom{\'e}dica (INEB), Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: ccbarrias@ineb.up.ptChemicals/CAS: alginic acid, 28961-37-7, 29894-36-8, 9005-32-7, 9005-38-3; calcium alginate, 9005-35-0; glucosylceramidase, 37228-64-1; iodine 125, 14158-31-7, 22822-81-7; Alginates; alginic acid, 9005-32-7; Drug Carriers; Enzymes, Immobilized; Glucosylceramidase, EC 3.2.1.45; Glucuronic Acid, 576-37-4; Hexuronic AcidsManufacturers: GenzymeReferences: Grabowski, G.A., Leslie, N., Wenstrup, R., Enzyme therapy for Gaucher disease: The first 5 years (1998) Blood Rev, 12, pp. 115-133;Zhao, H., Grabowski, G.A., Gaucher disease: Perspectives on a prototype lysosomal disease (2002) Cell Mol Life Sci, 59, pp. 694-707; 
Friedman, B., Vaddi, K., Preston, C., Mahon, E., Cataldo, J.R., McPherson, J.M., A comparison of the pharmacological properties of carbohydrate remodeled recombinant and placental-derived beta-glucocerebrosidase: Implications for clinical efficacy in treatment of Gaucher disease (1999) Blood, 93, pp. 2807-2816; 
Rasmussen, J., Barsomian, G., Bergh, M., Enzymatically active recombinant glucocerebrosidase. U.S. patent 6451600. 17 September 2002Elstein, D., Itzchaki, M., Mankin, H.J., Skeletal involvement in Gaucher{\textquoteright}s disease (1997) Baillieres Clin Haematol, 10, pp. 793-816; 
Wenstrup, R.J., Roca-Espiau, M., Weinreb, N.J., Bembi, B., Skeletal aspects of Gaucher disease: A review (2002) Br J Radiol, 75 (SUPPL. 1), pp. A2-A12; 
Mistry, P.K., Wraight, E.P., Cox, T.M., Therapeutic delivery of proteins to macrophages: Implications for treatment of Gaucher{\textquoteright}s disease (1996) Lancet, 348, pp. 1555-1559; 
Gregoriadis, G., Neerunjun, D., Meade, T.W., Goolamali, S.K., Weereratne, H., Bull, G., Experiences after long-term treatment of a type I Gaucher disease patient with liposome-entrapped glucocerebroside: Beta-glucosidase (1980) Birth Defects Orig Artic Ser, 16, pp. 383-392; 
Dale, G.L., Kuhl, W., Beutler, E., Incorporation of glucocerebrosidase into Gaucher{\textquoteright}s disease monocytes in vitro (1979) Proc Natl Acad Sci USA, 76, pp. 473-475; 
Beutler, E., Dale, G.L., Guinto, D.E., Kuhl, W., Enzyme replacement therapy in Gaucher{\textquoteright}s disease: Preliminary clinical trial of a new enzyme preparation (1977) Proc Natl Acad Sci USA, 74, pp. 4620-4623; 
Belchetz, P.E., Crawley, J.C., Braidman, I.P., Gregoriadis, G., Treatment of Gaucher{\textquoteright}s disease with liposome-entrapped glucocerebroside: Beta-glucosidase (1977) Lancet, 2, pp. 116-117; 
Korablyov, V., Zimran, A., Barenholz, Y., Cerebroside-beta-glucosidase encapsulation in liposomes for Gaucher{\textquoteright}s disease treatment revisited (1999) Pharm Res, 16, pp. 466-469; 
Busto, M.D., Ortega, N., Perez-Mateos, M., Effect of immobilization on the stability of bacterial and fungal beta-glucosidase (1997) Process Biochem, 32, pp. 441-449; 
Dashevsky, A., Protein loss by the microencapsulation of an enzyme (lactase) in alginate beads (1998) Int J Pharm, 161, pp. 1-5; 
Blandino, A., Macias, M., Cantero, D., Immobilization of glucose oxidase within calcium alginate gel capsules (2001) Process Biochem, 36, pp. 601-606; 
Kokufuta, E., Shimizu, N., Tanaka, H., Nakamura, I., Use of polyelectrolyte complex-stabilised calcium alginate gel for entrapment of beta-amylase (1988) Biotechnol Bioeng, 33, pp. 756-759; 
Edelman, E.R., Mathiowitz, E., Langer, R., Klagsbrun, M., Controlled and modulated release of basic fibroblast growth factor (1991) Biomaterials, 12, pp. 619-626; 
Peters, M.C., Isenberg, B.C., Rowley, J.A., Mooney, D.J., Release from alginate enhances the biological activity of vascular endothelial growth factor (1998) J Biomater Sci Polym Ed, 9, pp. 1267-1278; 
Alsberg, E., Anderson, K.W., Albeiruti, A., Franceschi, R.T., Mooney, D.J., Cell-interactive alginate hydrogels for bone tissue engineering (2001) J Dent Res, 80, pp. 2025-2029; 
Rowley, J.A., Madlambayan, G., Mooney, D.J., Alginate hydrogels as synthetic extracellular matrix materials (1999) Biomaterials, 20, pp. 45-53; 
Gagne, T.A., Chappell-Afonso, K., Johnson, J.L., McPherson, J.M., Oldham, C.A., Tubo, R.A., Vaccaro, C., Vasios, G.W., Enhanced proliferation and differentiation of human articular chondrocytes when seeded at low cell densities in alginate in vitro (2000) J Orthop Res, 18, pp. 882-890; 
(1993) Iodine-125. A Guide to Radioiodination Techniques: Amersham Life Science, , Amersham Place, Little Chalfont, Bucks: Amersham International pic; 64 pp; 
Sa Miranda, M.C., Aerts, J.M., Pinto, R., Fontes, A., De Lacerda, L.W., Van Weely, S., Barranger, J., Tager, J.M., Activity of glucocerebrosidase in extracts of different cell types from type 1 Gaucher disease patients (1990) Clin Genet, 38, pp. 218-227; 
Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Klenk, D.C., Measurement of protein using bicinchoninic acid (1985) Anal Biochem, 150, pp. 76-85; 
Sa Miranda, M.C., Aerts, J.M., Pinto, R.A., Magalhaes, J.A., Barranger, J.A., Tager, J.M., Schram, A.W., Heterogeneity in human acid beta-glucosidase revealed by cellulose-acetate electrophoresis (1988) Biochim Biophys Acta, 965, pp. 163-168; 
Smidsrod, O., Draget, K.I., Chemistry and physical properties of alginates (1996) Carbohyd Eur, 14, pp. 6-13; 
Gaserod, O., Sannes, A., Skjak-Braek, G., Microcapsules of alginate-chitosan. II. A study of capsule stability and permeability (1999) Biomaterials, 20, pp. 773-783; 
Aslani, P., Kennedy, R.A., Studies on diffusion in alginate gels. I. Effect of cross-linking with calcium or zinc ions on diffusion of acetaminophen (1996) J Control Release, 42, pp. 75-82
},
	month = {2005///},
	pages = {545 - 552},
	abstract = {Gaucher disease (GD) is caused by the decreased activity and/or stability of the lysosomal enzyme glucocerebrosidase (GCR). The available treatment consists in the intravenous administration of exogenous GCR, and is effective in reverting most of the symptoms. However, in terms of bone pathology, which is among the most disabling manifestations, a slow and incomplete response is observed, indicating that adjuvant therapies are necessary to consistently restore GCR activity in bone and accelerate regeneration. In this study, calcium alginate microspheres were analyzed as a vehicle for localized GCR delivery to bone. Results demonstrated that the entrapped enzyme retained full activity and exhibited a broader pH-dependent activity profile, compared to that of free-GCR, with improved stability at physiological pH. GCR release profile was established, and it was demonstrated that GCR could be released in a sustained manner. The biological behavior of the system was evaluated by analyzing the uptake of released GCR by GCR-deficient cells from GD patients, using different techniques: GCR activity measurements, radiolabeling, and cellulose acetate electrophoresis. Results demonstrated that GCR was internalized by cells significantly enhancing the residual enzymatic activity. To achieve an activity reconstitution level comparable to that obtained using free-GCR, only half of the dose was required with entrapped-GCR. {\textcopyright} 2005 Wiley Periodicals, Inc.},
	keywords = {Alginates, alginic acid, article, Bone, bone disease, Bone Regeneration, Calcium alginate, Calcium Compounds, catalysis, Cell culture, Cells, Cultured, controlled study, Drug Carriers, drug delivery system, enzyme activity, enzyme assay, enzyme replacement, Enzymes, Enzymes, Immobilized, fibroblast culture, Fibroblasts, Gaucher disease, Gaucher disease (GD), Glucocerebrosidase (GCR), Glucosylceramidase, Glucuronic Acid, Hexuronic Acids, human, human cell, Humans, iodine 125, Localized delivery, lysosome enzyme, lysosome storage disease, microsphere, Microspheres, Pathology, pH effects, physiology, recombinant enzyme, Therapeutic enzyme},
	isbn = {00219304 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-24044465170\&partnerID=40\&md5=bbcee8568e0c0223975853a8177439c8},
	author = {Barrias, C.C. and Lamghari, M. and Granja, P.L. and S{\'a} Miranda, M.C. and Barbosa, M.A.}
}
@article {2482,
	title = {Fabrication of alternating polycation and albumin multilayer coating onto stainless steel by electrostatic layer-by-layer adsorption},
	journal = {Colloids and Surfaces B: BiointerfacesColloids Surf. B Biointerfaces},
	volume = {34},
	year = {2004},
	note = {Cited By (since 1996): 17Export Date: 21 November 2012Source: ScopusCODEN: CSBBEdoi: 10.1016/j.colsurfb.2003.12.015PubMed ID: 15261073Language of Original Document: EnglishCorrespondence Address: Ji, J.; Department of Polymer Science, Zhejiang University, Hangzhou 310027, China; email: jianji@mail.hz.zj.cnChemicals/CAS: iodine 125, 14158-31-7, 22822-81-7; polyethyleneimine, 74913-72-7; stainless steel, 12597-68-1; Albumins; Lipid Bilayers; Polyamines; polycations; Polyethyleneimine, 9002-98-6; Stainless Steel, 12597-68-1References: Thomann, U.I., Uggowitzer, P.J., (2000) Wear, 239, p. 48;Cheatham, J., (2001) Prog. Pediat. Cardiol., 14, p. 95; 
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Ladam, G., Schaaf, P., Cuisinier, F.J.G., Decher, G., Voegel, J.C., (2001) Langmuir, 17, p. 878; 
Bertrand, P., Jonas, A., Laschewsky, A., Legras, R., (2000) Macromol. Rapid Commun., 21, p. 319
},
	month = {2004///},
	pages = {185 - 190},
	abstract = {Multilayer films consisting of polyethylenimine (PEI) and albumin were successfully prepared on biomedical 316L stainless steel surface via electrostatic self-assembly of the PEI and albumin. The process of electrostatic self-assembly of PEI/albumin was monitored by                        125I radiolabeling, electrochemical impedance spectroscopy (EIS) and atomic force microscopy (AFM). The EIS data revealed that the multilayer coating was stable in Tris-HCl (pH 7.35) buffer solution for 21 days. 
                        125I radiolabeling experiments indicated that less than 10\% albumin was eluted by PBS in 45 days. Static platelet adhesion experiments indicated that the PEI/albumin deposited on stainless steel could resist platelet adhesion effectively. Such an easy processing and shape-independent method may have good potential for surface modification of cardiovascular devices. {\textcopyright} 2004 Elsevier B.V. All rights reserved.
},
	keywords = {Adhesion, Adsorption, Albumin, Albumins, article, Atomic force microscopy, Cardiovascular devices, Chemical modification, Coatings, Electric Impedance, Electric Potential, Electrochemical impedance spectroscopy, electrochemistry, Electrons, Electrostatics, film coating, iodine 125, isotope labeling, Layer-by-layer, Lipid Bilayers, Microscopy, Atomic Force, Multilayers, Nonthrombogenic, pH effects, Platelet Adhesiveness, Polyamines, polycation, Polycations, Polyethyleneimine, priority journal, Proteins, Self assembly, Spectroscopy, Spectrum Analysis, Stainless steel, Surface modification, Surface Properties, surface property, Surface treatment, thrombocyte adhesion},
	isbn = {09277765 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-1642271404\&partnerID=40\&md5=29885596e6efdc7afcc5b2fdd57317be},
	author = {Ji, J. and Tan, Q. and Fan, D.-Z. and Sun, F.-Y. and Barbosa, M.A. and Shen, J.}
}
@book {2476,
	title = {Protein adsorption effect on in vitro acellular biodegradation of CaO-P                    2O
                    5 glass ceramics
},
	series = {Materials Science ForumMater Sci Forum},
	volume = {455-456},
	year = {2004},
	note = {Conference code: 63332Cited By (since 1996): 2Export Date: 21 November 2012Source: ScopusCODEN: MSFOELanguage of Original Document: EnglishCorrespondence Address: Santos, J.D.; Inst. de Engenharia Biom{\'e}dica, Laborat{\'o}rio de Biomateriais, Rua do Campo Alegre, 823, 4150-180 Porto, Portugal; email: jdsantos@fe.up.ptReferences: Zeng, Chittur, K.K., Lacefield, W.R., (1999) Biomaterials, 20, p. 377;Ohta, Monna, H., Takahashi, S., (2001) J. Biomed. Mater. Res., 55, p. 409; 
Zyman, Z., Dedukh, N.V., Glusko, V.I., Shcherbyna, S.V., (2002) 17 th European Society for Biomaterials Conference Proceedings, , Barcelona; 
Krajewski, Malavoti, R., Piancatelli, A., (1996) Biomaterials, 17, p. 53; 
El-Ghannam, Ducheyne, P., Shapiro, I.M., (1997) Biomaterials, 18 (4); 
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Dubois, C., Souchier, C., Couble, M.L., Exbrayat, P., Lissac, M., (1999) Biomat., 20, p. 1841; 
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Dias, G., Lopes, M.A., Gibson, I.R., Santos, J.D., (2002) 17 th Europ. Soc. for Biomat. Conf. Proc., , Barcelona; 
Chun, Na, S.W., Lee, J.H., Chung, J.P., Ryu, I.C., Kim, S.Y., (2002) Key Eng. Mat., 218-220, p. 149
},
	month = {2004///},
	pages = {398 - 401},
	address = {Caparica},
	abstract = {This work reports the in vitro accelular behaviour of a glass ceramic (45P                        2O
                        5-45CaO-5MgO-5K
                        2O), which has significant potential for being used as an alloplastic bone graft. Experiments were carried out by immersing granule samples for a period up to 90 days in Trisbuffer solution at pH 7.4, in the presence and absence of a foetal bovine serum (FBS). The release of calcium, phosphorus, and potassium ions as well as the amount of protein adsorbed was followed by several techniques. The results obtained seem to indicate that the adsorption of proteins on the surface of the material, although causing an initial delay in the degradation, does not hamper the ionic exchange and therefore it is not a barrier for the degradation of the glass ceramic.
},
	keywords = {Adsorption, Bioceramics, Biodegradation, Calcium Compounds, Foetal bovine serum (FBS), Glass ceramics, Hard tissue, Ion exchange, Ionic strength, pH effects, Protein adhesion, Proteins, Tissue},
	isbn = {02555476 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-3142740181\&partnerID=40\&md5=5452672cf92db3be0d9f232ce3b1a83e},
	author = {Dias, A.G. and Lopes, M.A. and Santos, J.D.},
	editor = {Martins R. and Fortunato E. and Ferreira I. and Dias C.}
}
@article {2593,
	title = {In vitro biomineralization by osteoblast-like cells II. Characterization of cellular culture supernatants},
	journal = {BiomaterialsBiomaterials},
	volume = {19},
	year = {1998},
	note = {Cited By (since 1996): 7Export Date: 21 November 2012Source: ScopusCODEN: BIMADdoi: 10.1016/S0142-9612(97)00150-6PubMed ID: 9678846Language of Original Document: EnglishCorrespondence Address: Carvalho, G.S.; IEC, Universidade do Minho, Largo do Paco, 4719 Braga Codex, PortugalChemicals/CAS: Calcium, 7440-70-2; Chromium, 7440-47-3; Culture Media; Iron, 7439-89-6; Metals; Nickel, 7440-02-0; Phosphorus, 7723-14-0; Stainless Steel, 12597-68-1References: Pereira, M.L., Silva, A., Tracana, R., Carvalho, G.S., Toxic effects caused by stainless steel corrosion products on mouse seminiferous cells (1994) Cytobios, 77, pp. 73-80;Pereira, M.L., Abreu, A.M., Sousa, J.P., Carvalho, G.S., Chromium accumulation and ultrastructural changes in the mouse liver caused by stainless steel corrosion products (1995) J Mater Sci Mater Med, 6, pp. 523-527; 
Tracana, R.B., Pereira, M.L., Abreu, A.M., Sousa, J.P., Carvalho, G.S., Stainless steel corrosion products cause alterations on mouse spleen cellular populations (1995) J Mater Sci Mater Med, 6, pp. 56-61; 
Bravo, I., Sousa, S.R., Carvalho, G.S., Barbosa, M., Metals electrochemically dissolved in human serum inhibit T-lymphocyte function (1992) Advances in Biomaterials, pp. 7-11. , Doherty PJ, et al., editors. Amsterdam: Elsevier; 
Carvalho, G.S., Castanheira, M., Diogo, I., Inhibition and stimulation of enzymatic activities of human fibroblasts by corrosion products and metal salts (1995) J Mater Sci Mater Med, 7, pp. 77-83; 
Morais, S., Sousa, J.P., Fernandes, M.H., Carvalho, G.S., In vitro bone formation in the presence of stainless steel corrosion products (1994) Poster Section, 11th European Conference on Biomaterials, , Pisa, Italy; 
Sousa, J.P., Requirements in materials for biosensors J Mater Sci Mater Med, , in press; 
Morais, S., Sousa, J.P., Fernandes, M.H., Carvalho, G.S., In vitro biomineralisation by osteoblast like cells. I. Retardation of tissue mineralisation by metal salts (1998) Biomaterials, 19, pp. 13-21; 
Morais, S., Carvalho, G.S., Sousa, J.P., Determination of nickel in osteoblast-like cell culture medium by adsorptive cathodic stripping voltammetry with mercury microelectrodes (1997) Electroanalysis, 9 (5), pp. 422-426; 
Morais, S., Carvalho, G.S., Sousa, J.P., Optimization study for nickel quantification in cell culture medium using mercury film microelectrodes (1996) Portugaliae Electrochimica Acta, 14, pp. 267-272; 
Morais, S., Carvalho, G.S., Sousa, J.P., Iron determination in osteoblast-like cell culture medium by adsorptive cathodic stripping voltammetry with a mercury microelectrode (1997) Electroanalysis, 9, pp. 791-795; 
Morais, S., Carvalho, G.S., Sousa, J.P., Chromium determination in osteoblast-like cell culture medium by catalytic stripping voltammetry with a mercury microelectrode Electroanalysis, , submitted for publication; 
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},
	month = {1998///},
	pages = {23 - 29},
	publisher = {Elsevier Sci Ltd},
	abstract = {The quantification of total calcium, phosphorus, iron, chromium and nickel in cell culture medium by electrochemical or spectroscopic means may require digestion of samples. Nevertheless, when pH adjustment is performed for values higher than about 6.5, the formation of two phases occurs: a white precipitate and a clear solution. Analysing both phases using microelectrodes, atomic absorption spectrometry (AAS), diffuse reflectance infrared Fourier transform (DRIFT) spectroscopy. X-ray dispersive (XRD) analysis, scanning electron microscopy (SEM) and energy dispersive spectroscopic (EDS) analysis, it was oberved that iron, chromium and nickel are not co-precipitating with the white solid phase. If quantification of calcium, phosphorus and magnesium is intended, a ten-fold dilution at least, must be performed to avoid most of these elements going into the precipitate. This knowledge is crucial if a mineralization study is going to be made.The quantification of total calcium, phosphorus, iron, chromium and nickel in cell culture medium by electrochemical or spectroscopic means may require digestion of samples. Nevertheless, when pH adjustment is performed for values higher than about 6.5, the formation of two phases occurs: a white precipitate and a clear solution. Analyzing both phases using microelectrodes, atomic absorption spectrometry (AAS), diffuse reflectance infrared Fourier transform (DRIFT) spectroscopy, X-ray dispersive (XRD) analysis, scanning electron microscopy (SEM) and energy dispersive spectroscopic (EDS) analysis, it was observed that iron, chromium and nickel are not co-precipitating with the white solid phase. If quantification of calcium, phosphorus and magnesium is intended, a ten-fold dilution at least, must be performed to avoid most of these elements going into the precipitate. This knowledge is crucial if a mineralization study is going to be made.
},
	keywords = {Absorption spectroscopy, Animals, article, atomic absorption spectrometry, Biomaterials, bone mineralization, Calcification, Physiologic, Calcium, Cell culture medium, Cells, Cultured, Chromium, Culture Media, culture medium, Diffuse reflectance infrared Fourier transform (DRIFT) spectroscopy, electrochemistry, Energy dispersive spectroscopic analysis, Fourier transform infrared spectroscopy, Hydrogen-Ion Concentration, infrared spectroscopy, Iron, Magnesium, Metals, microelectrode, Microelectrodes, Nickel, nonhuman, osteoblast, Osteoblast cells, Osteoblasts, pH effects, phosphorus, precipitation, Precipitation (chemical), priority journal, Rabbits, Scanning electron microscopy, Spectrophotometry, Atomic, Spectroscopic techniques, Spectroscopy, Stainless steel, supernatant, Supernatants, Tissue culture, X ray analysis, X ray dispersive analysis},
	isbn = {01429612 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0031841533\&partnerID=40\&md5=62f6b7869003505ce8adfdf96ca2a9f0},
	author = {Morais, S. and Carvalho, G.S. and Faria, J.L. and Gomes, H.T. and Sousa, J.P.}
}
@article {2629,
	title = {Modifications in the molecular structure of hydroxyapatite induced by titanium ions},
	journal = {Journal of Materials Science: Materials in MedicineJ. MATER. SCI. MATER. MED.},
	volume = {6},
	year = {1995},
	note = {Cited By (since 1996): 22Export Date: 21 November 2012Source: ScopusCODEN: JSMMEdoi: 10.1007/BF00134326Language of Original Document: EnglishCorrespondence Address: Ribeiro, C.C.; Instituto de Engenharia Biomedica, Praca do Coronel Pacheco, 1, 4050 Porto, Portugal},
	month = {1995///},
	pages = {829 - 834},
	publisher = {Chapman \& Hall Ltd},
	abstract = {The purpose of this study was to contribute to the understanding of the effect of titanium ions released from a metallic substrate on the molecular structure of hydroxyapatite. The effects of pH, time of incubation and concentration of titanium ions were investigated. The solids were analysed by X-ray diffraction, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, energy dispersive X-ray analysis and thermogravimetric analysis. The results clearly indicate the presence of a titanium phosphate, Ti(HPO                        4)
                        2{\textperiodcentered}nH
                        2O (n = 1-3), which probably has a double layered structure. The formation of this compound is dependent on the titanium concentration and its crystallinity increases with the time of incubation.
The purpose of this study was to contribute to the understanding of the effect of titanium ions released from a metallic substrate on the molecular structure of hydroxyapatite. The effects of pH, time of incubation and concentration of titanium ions were investigated. The solids were analysed by X-ray diffraction, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, energy dispersive X-ray analysis and thermogravimetric analysis. The results clearly indicate the presence of a titanium phosphate, Ti(HPO
                        4)
                        2{\textperiodcentered}nH
                        2O (n = 1-3), which probably has a double layered structure. The formation of this compound is dependent on the titanium concentration and its crystallinity increases with the time of incubation.
},
	keywords = {Calcium Compounds, Chemical structure, Coatings, conference paper, Crystallinity, Crystallization, Dissolution, Energy dispersive x ray analysis, Fourier transform infrared spectroscopy, Fourier transform Raman spectroscopy, hydroxyapatite, Implants (surgical), incubation time, infrared spectroscopy, Ions, metal ion, Molecular Structure, pH, pH effects, phosphate, Phosphates, priority journal, Raman spectrometry, Raman spectroscopy, Thermogravimetric analysis, thermogravimetry, time, Titanium, Titanium compounds, X ray analysis, X ray diffraction},
	isbn = {09574530 (ISSN)},
	url = {http://www.scopus.com/inward/record.url?eid=2-s2.0-0029583899\&partnerID=40\&md5=724de7ed1c6fddd7a7e258cd19ba3710},
	author = {Ribeiro, C.C. and Barbosa, M.A. and Machado, A.A.S.C. and Tudor, A. and Davies, M.C.}
}
