Solon A. Ellison

THE PROTEINS OF HUMAN PAROTID AND SUBMAXILLARY SALIVA

Electrophoretic and ultracentrifugal studies of parotid and submaxillary secretions have shown the presence of a number of protein components? Immunological examinations of saliva with antisaliva sera and antisera to serum proteins have indicated the presence of serum albumin and globulins as well as a group of intrinsic salivary proteins of which amylase is the dominant member.2-4 To date, however, only the amylase has been fully characterized. The large body of work on submaxillary mucoids has been confined almost exclusively to cattle gland extracts, and little is known about the mucoids as they exist in the secretion. One of the major problems in characterizing the salivary proteins is the paucity of procedures for separating substantial amounts of the various components. Preliminary work with diethylaminoethyl cellulose and apatite column chromatography shows p ro~n i se ,~ ,~ but now paper electrophoresis seems to give the maximal separation. Although the relatively small amount of material available from eluates limits the procedures that can be used for examination of the separated fractions, valuable information has been gained.

The Isolation of a Family of Cysteine-containing Phosphoproteins from Human Submandibular-Sublingual Saliva

A family of acidic proteins has been isolated from human submandibular-sublingual saliva using Sephadex G-200 gel filtration, DE-52 cellulose chromatography, and immuno-affinity chromatography. These molecules were homogenous in size and by immunological criteria, but exhibited charge heterogeneity. The heterogeneity displayed was not due to gustatory stimulation or degradation during isolation procedures.

Characterization of Cysteine-containing Phosphoproteins from Human Submandibular-Sublingual Saliva

Members of a family of acidic proteins taken from human submandibular-sublingual saliva were designated cysteine-containing phosphoproteins, since they could be distinguished from other salivary phosphoproteins by the presence of half-cystine. These molecules consisted of a single peptide chain of ~ 14,000 daltons. Their isoelectric points ranged from 4.3 to 5.9. Two groups (C2 and C3) were 0-phosphorylated. Their charge heterogeneity was apparently due to variations in content of phosphate and acidic and basic amino acids.

Serial sections of vaccinia virus examined at one stage of development in the electron microscope

Abstract Two clusters of intracytoplasmic viral particles are illustrated in eight consecutive serial sections. The sections average 30–33 mμ in thickness. The viral particles are spherical with diameters varying from 200–240 mμ. They possess a dense, limiting membrane 9–12 mμ thick. All particles sectioned five or more times can be shown to contain a nucleoid at one stage of development.

Carbohydrate components of supragingival salivary calculus.

Summary Analysis of supragingival salivary calculus disclosed many similarities in composition to urinary and submaxillary gland calculus. All the carbohydrates reported to be present in the latter concretions were found in the supragingival material. In addition the supragingival salivary calculus contained small amounts of sialic acid, xylose and arabinose. From the nature of the carbohydrate components it would appear that both saliva and bacteria contribute to the composition of supragingival salivary calculus.