muramidase has been researched along with fluorapatite* in 2 studies
2 other study(ies) available for muramidase and fluorapatite
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Protein films adsorbed on experimental dental materials: ToF-SIMS with multivariate data analysis.
The proteins lysozyme, amylase, and bovine serum albumin (BSA) were adsorbed on two experimental dental materials, made of fluoroapatite particles embedded in polymer matrices, and on silicon wafers. The protein films were prepared as single-component layers, as binary mixtures, and as double layers. These systems were investigated by time-of-flight secondary ion mass spectrometry (ToF-SIMS) and the multivariate data analysis technique of discriminant principal-component analysis (DPCA). During adsorption of a single protein film on to the solid surfaces, the three proteins could be clearly distinguished by the scores of their mass spectra after selection of amino acid-related peaks and DPCA. Furthermore, very similar results were obtained on the two different fluoroapatite substrates. For samples coated with binary layers of two proteins adsorbed simultaneously, it was found for both substrate types that BSA shows the strongest ability to adsorb followed by lysozyme, while amylase has the smallest ability. By contrast, the consecutive adsorption of two protein layers showed a strong influence of substrate type on the adsorption ability of the proteins. Topics: Adsorption; Amylases; Animals; Apatites; Cattle; Dental Materials; Discriminant Analysis; Humans; Multivariate Analysis; Muramidase; Serum Albumin, Bovine; Silicon; Spectrometry, Mass, Secondary Ion | 2008 |
Influence of fluoride applications on some physicochemical surface properties of synthetic hydroxyapatite and human dental enamel and its consequences for protein adsorption.
Synthetic hydroxyapatite and human dental enamel (polished and non-polished) were subjected to various fluoride applications, i.e., using solutions of sodium fluoride (NaF), acidulated phosphate fluoride (APF), and stannous fluoride (SnF2). Treatment with APF has a strong influence on the morphology of the apatite. All fluorides, in particular SnF2, make the enamel surfaces more hydrophobic. NaF and APF applications slightly alter the electrokinetic potentials of the surfaces, but SnF2 renders them much more negatively charged. The adsorption of the proteins lysozyme and alpha-lactalbumin on these surfaces can be explained in terms of electrostatic and hydrophobic interactions between the proteins and the sorbent surfaces. Topics: Acidulated Phosphate Fluoride; Adsorption; Apatites; Dental Enamel; Durapatite; Electrochemistry; Fluorides, Topical; Humans; Lactalbumin; Microscopy, Electron, Scanning; Muramidase; Salivary Proteins and Peptides; Sodium Fluoride; Surface Properties; Tin Fluorides; Wettability | 1995 |