Proteins In Parotid Saliva Research Articles

Fractionation of human parotid saliva proteins.

A chromatographic procedure for purification of the proteins in human parotid saliva has been developed. The eluates of a Sephadex G-150 and two ion exchange columns have been analyzed simultaneously by several physical and chemical tests; these include three optical properties of proteins, assays for neutral sugars, sialic acid and zinc, and disc gel electrophoresis. The ratios of the different variables have been used to determine the homogeneity and complexity of the protein distribution in the various peaks of the chromatographic eluates. By chromatographic methods, it has been possible to purify a glycoprotein with unusual staining characteristics and amino acid composition. Glycoproteins with similar properties comprise a major portion of the proteins in parotid saliva and appear to constitute a family of related proteins which differ in molecular size, carbohydrate and sialic acid content, and electrophoretic mobility. The fractionation of several enzymes in parotid saliva is also reported.

Differential effect of autonomic stimulation on salivary secretion of IgG, IgA and amylase.

SummaryStimulation of the rat parotid gland was effected by pilocarpine administration immediately following removal of one superior cervical ganglion and saliva was collected from the denervated gland and contra-lateral neurally intact mate. In this fashion it was possible to evaluate the effects of sympathetic and parasympathetic stimulation on the secretory responses of several proteins in parotid saliva. The flow rate of saliva obtained with cholinergic stimulation was higher than that with adrenergic stimulation. On the other hand, stimulation of adrenergic receptors caused secretion of total protein and amylase from the gland, in appreciably higher concentration than that elicited in response to cholinergic stimulation. Amylase level in secretion obtained from the neurally intact parotid gland immediately following pilocarpine injection was about 20 times that of the sympathectomized gland and gradually decreased with time reaching a level of about 4 times that of the denervated mate after 45 min. T...

Colloid and Crystal Formation in Parotid Saliva of Cystic Fibrosis Patients and Non-Cystic Fibrosis Subjects. I. Physicochemistry

Two types of turbidity were found in parotid saliva from both cystic fibrosis (CF) patients and non-CF subjects. On cooling saliva, a rapidly forming, reversible, cold-dependent turbidity appeared in increasing amounts with decreasing temperature and increasing protein concentration. At 37 degrees, a slowly forming, stable turbidity appeared in increased amounts in parotid saliva samples containing increased amounts of calcium. The 2 degree centrifuged pellet consisted predominantly of protein, whereas the 37 degree pellet contained calcium, inorganic phosphate, and protein. The cold-dependent turbidity at 2 degrees was not inhibited by EDTA, but 37 degrees turbidity was dramatically inhibited. Urea and guanidine hydrochloride reduced 2 degree turbidity, and, to a lesser extent, inhibited 37 degree turbidity. The tendency towards higher levels of protein, amylase, and calcium in CF compared with child control parotid saliva (4, 6) causes a greater incidence and degree of turbidity formation in saliva of CF patients. In this paper only the nature of the turbidity has been investigated, not its relative occurrence in each group of subjects.

Polyacrylamide gel patterns of parotid saliva proteins in Caucasoids and Amerindians

Parotid saliva protein samples collected from 69 Caucasoid and 71 Amerindian (Crow Indian Reservation, Montana) donors were subjected to polyacrylamide gel slab electrophoresis, pH 9.0. Coomassie Blue staining revealed a total of 36 distinguishable protein bands at equivalent positions on the gels from samples of both the Caucasoids and Amerindians. Marked variability of parotid protein patterns among both Caucasoids and Amerindians was evident. Seven bands were present in a significantly greater ( p < 0.05 − p < 0.005) proportion of Caucasoid samples, while one band was present in a significantly greater ( p < 0.005) proportion of Amerindian patterns. The average number of protein bands detected in the Amerindian patterns was significantly fewer ( p < 0.005) than that of Caucasoids. “Proline-rich” proteins were detected on additional gels of samples from both Caucasoids and Amerindians. Distinct variability among individuals from both groups was evident also in the occurrence of “proline-rich” parotid proteins. Reactions (bands) indicating “proline-rich” proteins were observed at 10 positions on gels from Caucasoid samples. Significantly fewer ( p < 0.005) “proline-rich” areas were detected on gels from Amerindian than Caucasoid saliva. Four of the “proline-rich” bands were present in a significantly greater ( p < 0.05 − p < 0.005) proportion of Caucasoid than Amerindian patterns. It is concluded that there are not consistent specific differences in parotid saliva protein composition between Caucasians and Amerindians. However, the proportion of subjects in which certain protein bands occur, following separation of the protein by polyacrylamide gel electrophoresis, differs between the two populations.

Amylase and protein in parotid saliva after load doses of different dietary carbohydrates

Parotid saliva was collected from seven young women after a 12-hr fast and 1 and 2 hr after load doses of seven different carbohydrates and after water alone. Total protein, amylase activity, flow rate, protein patterns on polyacrylamide gel, and recovery of amylase activity from the gel were investigated. Amylase and total protein secretion increased 1 and 2 hr after the carbohydrate load dose and after water alone. The increase could not be attributed to the carbohydrate load doses. Correlation between amylase activity and total protein was highly significant. No correlation was found between flow rate and amylase activity or protein content in parotid saliva, or between flow rate and the different carbohydrate load doses. Parotid amylase activity and total protein secretion varied greatly, both among and within the seven subjects. Considerable variation was noted in the flow rate between the subjects, but the flow rate for each subject was relatively constant throughout the study. Unconcentrated parotid saliva separated on polyacrylamide gels typically showed six to seven protein areas with one major amylolytic area after 60 min of electrophoresis. The area containing amylase activity further separated into three to four bands after 120 min of electrophoresis. The number of protein bands on the gels, which varied from subject to subject, did not appear to be affected by the kind of carbohydrate administered in a load dose.

Quantitative determination of protein in saliva

abstract – Seven methods for quantitative protein analysis were evaluated for the analysis of protein in saliva. The degree of interference from dialyzable components and from components retarded on Sephadex G‐50 was determined. Parotid saliva protein was fractionated into a glycoprotein‐rich and an amylase‐rich fraction on Sephadex G‐75, and the relative contributions from these protein fractions in the various protein tests were compared. Ultraviolet absorption at 215 mμ was recommended for the determination of total protein in salivary samples.

Zone electrophoresis of human parotid saliva in various media

A comparison has been made between the separations of the proteins of parotid saliva achieved by various methods of zone electrophoresis. A combination of two of these methods in the cellulose acetate/starch gel two-dimensional technique yields the most reproducible and informative results. Unidimensional starch gel electrophoresis is best suited for routine analysis, but where comparison with results from filter paper or cellulose acetate is required, the two-dimensional technique is essential. Electrophoresis on filter paper or cellulose acetate alone gives poor separation because of spreading and overlapping bands which can, however, be separated in starch gel.