[Electron paramagnetic resonance in polymethyl methacrylate irradiated with Co60].
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Polymethyl methacrylate bone cement is tested at the Institute of Fracture and Solid Mechanics Laboratory, Lehigh University. Standard tensile coupon and compact tension specimens are molded under varying conditons of temperature and pressure. Test results are obtained for the strength and toughness of bone cement involved in total hip replacement operations.
Raman spectroscopy provides valuable information on the physicochemical properties of hard tissues. While the technique can analyze tissues in their native state, analysis of fixed, embedded, and sectioned specimens may be necessary on certain occasions. The information on the effects of fixatives and embedding media on Raman spectral properties is limited. We examined the effect of ethanol and glycerol as fixatives and a variety of embedding media (Araldite, Eponate, Technovit, glycol methacrylate, polymethyl methacrylate, and LR white) on Raman spectral properties (mineralization, crystallinity, and carbonation) measured from the cortical bone of mouse humeri. Humeri were fixed in ethanol or glycerol, followed by embedding in one of the media. Nonfixed, freeze-dried, and fixed but not embedded sections were also examined. Periosteal, endosteal, and midosteal regions of the intracortical envelope were analyzed. Raman spectra of fixative solutions and embedding media were also recorded separately in order to examine the specifics of overlap between spectra. We found significant effects of fixation, embedding, and anatomical location on Raman spectral properties. The interference of ethanol with tissue seemed to be relatively less pronounced than that of glycerol. However, there was no single combination of fixation and embedding that left Raman spectral parameters unaltered. We conclude that careful selection of a fixation and embedding combination should be made based on the parameter of interest and the type of tissue. It may be necessary to process multiple samples from the tissue, each using a combination appropriate for the Raman parameter in question.
PURPOSE: This study evaluated the effects of four adhesive primers on the shear bond strength of a self curing resin to cobalt-chromium alloy. MATERIAL AND METHODS: The adhesive primers Acryl Bond (AB), Cesead Opaque Primer (COP), Metal Primer II (MPII), and MR Bond (MRB) were used. A brass ring placed over the casting alloy disk surface nonprimed or primed with each primer was filled with the self-curing methyl methacrylate polymethyl methacrylate resin. The specimens were stored in water at 37 degrees C for 24 hours and then alternately immersed in water baths at 4 degrees C and 60 degrees C for 1 minute each for up to 20,000 thermal cycles before shear mode testing at a crosshead speed of 0.5 mm/min. RESULTS: All the primers examined improved the shear bond strength between the resin and cobalt chromium alloy compared with nonprimed specimens before thermal cycling. However, after 20,000 thermal cycles, the bond strengths of resin to cobalt chromium alloy primed with COP or MPII primers were significantly greater than those of specimens primed with AB or MRB primers and nonprimed controls. CONCLUSION: This study indicated that COP and MPII are effective primers to obtain higher bond strength between resin and cobalt-chromium alloy.
Polymethyl methacrylate (PMMA) films were treated by oxygen plasma discharge followed by acrylic acid (AA) grafting. The amount of carboxyl groups introduced by the grafting of AA on to the film surfaces was in the range 0.47-9.48 mumol/cm2, depending on the pressure of the plasma chamber during the discharge treatment. The carboxyl groups of the PMMA film surface previously activated with water soluble carbodiimide were coupled with bovine serum albumin, collagen and gelatin. The protein immobilization on the surface was confirmed by attenuated total reflection Fourier transform infra-red spectroscopy (ATR-FTIR) and electron spectroscopy for chemical analysis (ESCA). The amount of albumin, collagen and gelatin immobilized on the PMMA surface was 6.25, 7.25 and 13.75 micrograms/cm2, respectively, as determined by the coomassie brilliant blue-protein interaction. The water contact angle of the PMMA film was markedly decreased by oxygen plasma treatment, AA grafting or protein immobilization, indicating the increase of hydrophilicity of the surface-modified PMMA films. The protein-immobilized PMMA films may be widely used as a biocompatible material.