In vitro sorption of albumin, immunoglobulin G, and lysozyme to enamel and cementum from human teeth

Abstract

Sorption of three 125I-labeled human proteins (albumin, immunoglobulin G, and lysozyme) to enamel and cementum was investigated. All three proteins sorped most when suspended in 0.0005 M solution of phosphate or calcium chloride where the least competition between solute ions and label occurred. The addition of human serum to labeled proteins caused a decrease in their sorption which could be partially reversed by increasing the concentration of label. Kinetic experiments demonstrated that sorption was dependent on protein concentration and incubation time and that most of the sorption occurred within the first minute of the reaction. In conclusion, the binding of the three labeled proteins was affected by the charge of the solute ions and was dependent on ion concentration and reaction time. Sorption correlated for the most part with the pK values of the proteins and thus lysozyme, the most basic protein, sorped more than immunoglobulin G, which sorped more than albumin. In all cases, cementum bound more basic protein than did enamel. Increased levels of albumin sorption to enamel occurred when the protein was suspended in the CaCl2 solution rather than in phosphate. In addition, based on Scatchard analysis, approximately twice as many potential protein binding sites were found for cementum versus enamel.

Immunohistochemical investigation of the presence and distribution of cementum‐associated lipopolysaccharides in periodontal disease

“…Bravman, Everhardt & Stahl (1979) have previously used a rhodamine-labelled antibody technique to investigate the presence of cementum-associated antigens using autologous serum, but did not define the nature of the antigens or the antibodies in the sera. The interpretation of their results is also complicated by problems with auto- fluorescence of collagen, cementum and calculus and non-specific absorption of immunoglobulins to cementum (Fine, Wilton & Caravana 1984). These difficulties do not arise with the technique described here.…”

Effect of material characteristics and/or surface topography on biofilm development

“…This clearly indicates that the pellicle is formed by a selective adsorption of environmental macromolecules. The physicochemical surface properties of a pellicle, including its composition, packing, density, and/or configuration, are largely dependent on the physical and chemical nature of the underlying hard surface (Lee et al 1974;Baier & Glantz 1978;de Jong et al 1984;Fine et al 1984;Ruan et al 1986;Pratt-Terpstra et al 1989Rykke & Sonju 1991;Sipahi et al 2001). Thus, the characteristics of the underlying hard surface are transferred through the pellicle layers, and as such will still have its influence on the initial bacterial adhesion.…”

Enzymes in the acquired enamel pellicle

“…Lysozyme is an acidic protein (19). It reveals an antibody-independent defence function represented by muraminidase activity (70).…”

“…Lysozyme is also one of the main pellicle proteins (1,74). Lysozyme has been demonstrated to be present in the in situ-formed pellicles (12,40,42,44,74), as well as in experimental pellicles (15)(16)(17)(18)(19), in an active form. It remains intact when integrated into the in vivo-formed pellicle (55) and activity of the enzyme reaches a constant level after 5 min of pellicle formation in situ (12).…”

“…There are many publications that deal with enzymes in the pellicle. However, the majority of studies described were performed under in vitro conditions or with semiartificial substrates, such as hydroxyapatite beads or powder (4,(15)(16)(17)(18)(19)(20)(21). These substrates often possess surface properties that are different from those of human or bovine enamel, and reveal different water contact angles (22,23).…”