Human saliva is known to contain a number of enzymes and other protein constituents, but only one of these-salivary amylase-has been adequately characterized.\" 2 Electrophoretic data have indicated the presence of at least seven components, whose identity, deduced from such studies, must be considered largely conjectural.3-11 Immunochemical agar diffusion techniques 12'3 appear uniquely suitable to the problem of enumerating and identifying the antigenic substances in saliva. The results below are illustrative of those obtained by employing a plate diffusion technique and agar immunoelectrophoresis. By these means, several proteins have been distinguished, some of which have been identified as being serologically unaltered serum proteins.

Immunochemical Studies of Human Saliva. I. The Demonstration of Serum Proteins in Whole and Parotid Saliva

Characterization of salivary components separated by paper electrophoresis

The comparative biochemistry, physiology, and genetics of animal alpha-amylases.

Studies of the adsorption of human salivary proteins, in general, and the enzymes amylase, lysozyme, and neuraminidase, in particular, reveal that these proteins differ in their affinities for the surface of enamel. The enzymes studied retained their enzyme activity in the adsorbed state. Only amylase was desorbed by water; lysozyme was desorbed by its substrate; and all three enzymes, as well as most other adsorbed proteins, were desorbed by phosphate.

The Interaction of Salivary Proteins with Tooth Surface

Electrophoretic separations on paper: Past, present, and future-A review.

Organic constituents of human saliva vary around 0.5 g. per 100 ml. depending on the nature of the stimulus and the hour of collection. Most of the organic matter is protein, with mucin being the preponderant component. However, it is one of the smaller protein elements that has been the most widely studied, mainly because of its enzymatic action, that is, salivary amylase. Phase boundary electrophoresis studies have been reported by Blix2 on animal submaxillary mucin and by Bernfeld, Staub, and Fischer' and Muusu on human salivary amylase. In the present note, electrophoresis was carried out on whole human saliva. The method reported here is that of zone paper electrophoresis\"' 18M17 which utilizes filter paper as a matrix to support the buffer solution. This method offers the following advantages over the phase boundary-free solution technique of Tiselius.'5 1. By means of paper electrophoresis many determinations may be made with a volume needed for but a single sample in the phase boundary apparatus. 2. Less than 0.1 ml. samples will usually suffice for paper electrophoresis; with amounts this small, it is not possible to use phase boundary electrophoresis. 3. Optical transparency of samples is not necessary with paper electrophoresis. 4. Preparative dialysis against the buffer, which may induce degradative changes in complex materials such as saliva, is not a requirement because inorganic ions do not interfere with electrophoresis when using filter paper. 5. Separation of components by paper electrophoresis is more permanent than that produced by the phase boundary apparatus because the filter paper provides a matrix in which the protein elements are retained in their relative positions after completion of electrophoresis. 6. Enzyme migration may be traced after paper electrophoresis by testing sections of the filter paper with a suitable substrate for the specific

Thorn Kinersly

Papers

Preliminary paper electrophoretic study of saliva.

Paper electrophoretic study of some components of saliva.

An antibacterial effect of saliva demonstrated with use of paper electrophoresis.

Beta-track autoradiographic study of teeth with Ca45.