Abstract
This chapter contains the theory and protocols of experimental techniques used in this work, as well as details on the materials and methods for each experiment that was performed.
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References
Scorpio, R.: Fundamentals of Acids, Bases, Buffers and Their Application to Biochemical Systems. Kendall/Hunt Publishing Company (2000)
Förster, H.: Uv/Vis Spectroscopy. In Characterization I, pp 337–426. Springer (2004)
Koch, A.L.: Turbidity measurements of bacterial cultures in some available commercial instruments. Anal. Biochem. 38(1), 252–259 (1970)
Goodwin, T., Morton, R.: The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem. J. 40(5–6), 628 (1946)
Lakowicz, J.R.: Principles of Fluorescence Spectroscopy. Springer Science & Business Media (2013)
Bradford, M.M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72(1), 248–254 (1976)
Sober, H.A., Gutter, F.J., Wyckoff, M.M., Peterson, E.A.: Chromatography of proteins. Ii. Fractionation of serum protein on anion-exchange cellulose. J. Am. Chem. Soc. 78(4), 756–763 (1956)
Wu, C.-S.: Handbook of Size Exclusion Chromatography and Related Techniques: Revised and Expanded, vol. 91. CRC Press (2003)
Boyes, E., Gai, P.: Environmental high resolution electron microscopy and applications to chemical science. Ultramicroscopy 67(1), 219–232 (1997)
Brakenhoff, G., Blom, P., Barends, P.: Confocal scanning light microscopy with high aperture immersion lenses. J. Microscopy (Oxford) 117(2), 219–232 (1979)
Brenner, S., Horne, R.: A negative staining method for high resolution electron microscopy of viruses. Biochem. Biophys. Acta. 34, 103–110 (1959)
Hopwood, D.: Theoretical and practical aspects of glutaraldehyde fixation. Histochem. J. 4(4), 267–303 (1972)
Bancroft, J.D., Gamble, M.: Theory and Practice of Histological Techniques. Elsevier Health Sciences (2008)
Bernhard, W.: A new staining procedure for electron microscopical cytology. J. Ultrastruct. Res. 27(3), 250–265 (1969)
Daddow, L.: An abbreviated method of the double lead stain technique. J. Submicrosc. Cytol. 18(1), 221–224 (1986)
Pecora, R.: Dynamic light scattering measurement of nanometer particles in liquids. J. Nanopart. Res. 2(2), 123–131 (2000)
Goldburg, W.: Dynamic light scattering. Am. J. Phys. 67(12), 1152–1160 (1999)
O’Brien, R.W., White, L.R.: Electrophoretic mobility of a spherical colloidal particle. J. Chem. Soc. Faraday Trans. 2: Mol. Chem. Phys. 74, 1607–1626 (1978)
Miller, J.F., Schätzel, K., Vincent, B.: The determination of very small electrophoretic mobilities in polar and nonpolar colloidal dispersions using phase analysis light scattering. J. Colloid Interface Sci. 143(2), 532–554 (1991)
Hillenkamp, F., Karas, M., Beavis, R.C., Chait, B.T.: Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal. Chem. 63(24), 1193A–1203A (1991)
Opsal, R.B., Owens, K.G., Reilly, J.P.: Resolution in the linear time-of-flight mass spectrometer. Anal. Chem. 57(9), 1884–1889 (1985)
Hou, X., Jones, B.T.: Inductively coupled plasma‐optical emission spectrometry. Encyclopedia of Analytical Chemistry (2000)
Mercereau, J.: Superconducting magnetometers. Revue de physique appliquée 5(1), 13–20 (1970)
Clarke, J.: Principles and applications of squids. Proc. IEEE 77(8), 1208–1223 (1989)
Pykett, I.L., et al.: Principles of nuclear magnetic resonance imaging. Radiology 143(1), 157–168 (1982)
Bloembergen, N., Purcell, E.M., Pound, R.V.: Relaxation effects in nuclear magnetic resonance absorption. Phys. Rev. 73(7), 679 (1948)
Rehr, R.B., et al.: Improved in vivo magnetic resonance imaging of acute myocardial infarction after intravenous paramagnetic contrast agent administration. Am J. Cardiol. 57(10), 864–868 (1986)
Bydder, G., Hajnal, J., Young, I.: MRI: use of the inversion recovery pulse sequence. Clin. Radiol. 53(3), 159–176 (1998)
Okuda, M., Eloi, J.C., Sarua, A., Jones, S.E.W., Schwarzacher, W.: Energy barrier distribution for dispersed mixed oxide magnetic nanoparticles. J. Appl. Phys. 111(7) (2012)
Okuda, M., Eloi, J.-C., Jones, S.E.W., Sarua, A., Richardson, R.M., Schwarzacher, W.: Fe3o4 Nanoparticles: protein-mediated crystalline magnetic superstructures. Nanotechnology 23(41), 415601 (2012)
Danon, D., Skutelsk, E., Marikovs, Y., Goldstei, L.: Use of cationized ferritin as a label of negative charges on cell surfaces. J. Ultrastruct. Res. 38(5–6), 500–510 (1972)
Perriman, A.W., Cölfen, H., Hughes, R.W., Barrie, C.L., Mann, S.: Solvent-free protein liquids and liquid crystals. Angew. Chem. Int. Ed. 48(34), 6242–6246 (2009)
Fox, C.H., Johnson, F.B., Whiting, J., Roller, P.P.: Formaldehyde fixation. J. Histochem. Cytochem. 33(8), 845–853 (1985)
Fischer, A.H., Jacobson, K.A., Rose, J., Zeller, R.: Hematoxylin and eosin staining of tissue and cell sections. Cold Spring Harbor Protocols (5), pdb. prot4986 (2008)
Marshall, P., Horobin, R.: The mechanism of action of “Mordant” dyes—a study using preformed metal complexes. Histochemie 35(4), 361–371 (1973)
Waheed, A., Rao, K.S., Gupta, P.: Mechanism of dye binding in the protein assay using eosin dyes. Anal. Biochem. 287(1), 73–79 (2000)
Rosenberg, L.: Chemical basis for the histological use of safranin o in the study of articular cartilage. J. Bone Joint Surg. 53(1), 69–82 (1971)
Martin, I., Obradovic, B., Freed, L.E., Vunjak-Novakovic, G.: Method for quantitative analysis of glycosaminoglycan distribution in cultured natural and engineered cartilage. Ann. Biomed. Eng. 27(5), 656–662 (1999)
Kiernan, J.A.: Anionic counterstains. Cold Spring Harbor Protocols (7), pdb. top51 (2008)
Bruns, R.R., Palade, G.E.: Studies on blood capillaries Ii. Transport of ferritin molecules across the wall of muscle capillaries. J. Cell Biol. 37(2), 277–299 (1968)
Sundberg, D.R., Broman, H.: The application of the prussian blue stain to previously stained films of blood and bone marrow. Blood 10(2), 160–166 (1955)
Schöpf, B., et al.: Methodology description for detection of cellular uptake of PVA coated superparamagnetic iron oxide nanoparticles (Spion) in synovial cells of sheep. J. Magn. Magn. Mater. 293(1), 411–418 (2005)
Frank, M., Dapson, R., Wickersham, T., Kiernan, J.: Certification procedures for nuclear fast red (Kernechtrot), Ci 60760. Biotech. Histochem. 82(1), 35–39 (2007)
Sternberger, L.A., Hardy, P.H., Cuculis, J.J., Meyer, H.G.: The unlabeled antibody enzyme method of immunohistochemistry preparation and properties of soluble antigen-antibody complex (Horseradish Peroxidase-Antihorseradish Peroxidase) and its use in identification of spirochetes. J. Histochem. Cytochem. 18(5), 315–333 (1970)
Seligman, A.M., Karnovsky, M.J., Wasserkrug, H.L., Hanker, J.S.: Nondroplet ultrastructural demonstration of cytochrome oxidase activity with a polymerizing osmiophilic reagent, diaminobenzidine (Dab). J. Cell Biol. 38(1), 1–14 (1968)
Olsen, J.V., Ong, S.-E., Mann, M.: Trypsin cleaves exclusively c-terminal to arginine and lysine residues. Mol. Cell. Proteomics 3(6), 608–614 (2004)
Kurachi, K., Powers, J.C., Wilcox, P.E.: Kinetics of the reaction of chymotrypsin Aα with peptide chloromethyl ketones in relation to its subsite specificity. Biochemistry 12(4), 771–777 (1973)
Smythe, C.: The reaction of iodoacetate and of iodoacetamide with various sulfhydryl groups, with urease, and with yeast preparations. J. Biol. Chem. 114(3), 601–612 (1936)
Umezawa, H., AOYAGI, T., Morishima, H., Matsuzaki, M., Hamada, M., Takeuchi, T.: Pepstatin, a New Pepsin Inhibitor Produced by Agtinomygetes. J. Antibiotics 23(5), 259–262 (1970)
Diermayr, P., Kroll, S., Klostermeyer, H.: Influence of Edta and metal ions on a metalloproteinase from pseudomonas fluorescens biotype I. Bio. Chem. Hoppe-Seyler 368(1), 57–62 (1987)
Eyre, D.: Collagen of articular cartilage. Arthrit. Res. 4(1), 30–35 (2002)
Hollander, A.P., et al.: Increased damage to type ii collagen in osteoarthritic articular cartilage detected by a new immunoassay. J. Clin. Investig. 93(4), 1722 (1994)
Roughley, P.J., Lee, E.R.: Cartilage proteoglycans: structure and potential functions. Microsc. Res. Tech. 28(5), 385–397 (1994)
Müller, G., Hanschke, M.: Quantitative and qualitative analyses of proteoglycans in cartilage extracts by precipitation with 1, 9-Dimethylmethylene blue. Connect. Tissue Res. 33(4), 243–248 (1996)
Stone, J.E., Akhtar, N., Botchway, S., Pennock, C.A.: Interaction of 1, 9-Dimethylmethylene blue with glycosaminoglycans. Ann. Clin. Biochem.: Int. J. Biochem. Med. 31(2), 147–152 (1994)
Baeuerle, P.A., Huttner, W.B.: Chlorate–a potent inhibitor of protein sulfation in intact cells. Biochem. Biophys. Res. Commun. 141(2), 870–877 (1986)
Berridge, M.V., Tan, A.S.: Characterization of the cellular reduction of 3-(4, 5-Dimethylthiazol-2-Yl)-2, 5-Diphenyltetrazolium Bromide (Mtt): subcellular localization, substrate dependence, and involvement of mitochondrial electron transport in mtt reduction. Arch. Biochem. Biophys. 303(2), 474–482 (1993)
Candeias, L., MacFarlane, D.S., McWhinnie, S.W., Maidwell, N., Roeschlaub, C., Sammes, P.: The catalysed nadh reduction of resazurin to resorufin. J. Chem. Soc. Perkin Trans. 2(11), 2333–2334 (1998)
Decker, T., Lohmann-Matthes, M.-L.: A quick and simple method for the quantitation of lactate dehydrogenase release in measurements of cellular cytotoxicity and tumor necrosis factor (TNF) activity. J. Immunol. Methods 115(1), 61–69 (1988)
Pittenger, M.F., et al.: Multilineage potential of adult human mesenchymal stem cells. Science 284(5411), 143–147 (1999)
Ramirez-Zacarias, J., Castro-Munozledo, F., Kuri-Harcuch, W.: Quantitation of adipose conversion and triglycerides by staining intracytoplasmic lipids with oil red O. Histochemistry 97(6), 493–497 (1992)
Puchtler, H., Meloan, S.N., Terry, M.S.: On the history and mechanism of alizarin and Alizarin Red S stains for calcium. J. Histochem. Cytochem. 17(2), 110–124 (1969)
Aulthouse, A.L., et al.: Expression of the human chondrocyte phenotype in vitro. In Vitro Cell. Dev. Biol. 25(7), 659–668 (1989)
Grande, D., Halberstadt, C., Naughton, G., Schwartz, R., Manji, R.: Evaluation of matrix scaffolds for tissue engineering of articular cartilage grafts. J. Biomed. Mater. Res. 34(2), 211–220 (1997)
Freed, L.E., et al.: Biodegradable polymer scaffolds for tissue engineering. Biotechnol. (N Y). 12(7), 689–693 (1994)
Zuberer, D.A.: Recovery and enumeration of viable bacteria. Methods of Soil Analysis: Part 2—Microbiological and Biochemical Properties (methodsofsoilan2), pp. 119–144 (1994)
McFarland, J.: The nephelometer: an instrument for estimating the number of bacteria in suspensions used for calculating the opsonic index and for vaccines. J. Am. Med. Assoc. 49(14), 1176–1178 (1907)
Sutton, S.: Measurement of microbial cells by optical density. J. Valid. Technol. 17, 47–49 (2011)
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Correia Carreira, S. (2017). Materials and Methods. In: Rapid Cell Magnetisation Using Cationised Magnetoferritin. Springer Theses. Springer, Cham. https://doi.org/10.1007/978-3-319-60333-9_2
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DOI: https://doi.org/10.1007/978-3-319-60333-9_2
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