Fluoride in human parotid saliva.

Gustatory stimulation was used to collect parotid saliva in an ascending flow rate pattern. F concentration was found to be independent of rate of flow. The F level in unstimulated parotid saliva, collected before the stimulate samplings, was significantly (P less than 0.01) higher than that for the stimulated collections. It is suggested that this is an apparent increase based on the movement of water out of the lumen, which is in turn triggered by sodium reabsorption. The level of F in unstimulated saliva increased almost tenfold within one hour after the oral administration of 10 mg of F, and a significant (P less than 0.01) increase persisted even at 24 hours after administration of the dosage.     

Evaluation of kallikrein in human parotid and submandibular saliva

Saliva was collected from 10 subjects using a universal-design parotid collector and individually-adapted submandibular collectors. The enzymic activity of kallikrein was measured using D-leucylvalylarginine-p-nitroanilide as the substrate. Mean kallikrein activity was much higher in parotid saliva than in submandibular saliva; the difference was statistically significant. Protein concentrations were not significantly different, whereas alpha-amylase was, as expected, much higher in parotid saliva.     

Immuno-electrophoretic and chemical analyses of human parotid saliva

Dialyzed and lyophilized parotid saliva, collected from a single donor, was characterized with respect to its chemical composition and number of components. The number of components was determined by immuno-electrophoretic analysis, and these results compared with those obtained by zone electrophoresis in polyacrylamide. The carbohydrate content of parotid saliva consisted of 3.5 per cent fucose, 3.4 per cent N-acetylglucosamine, 3.1 per cent mannose, 2.6 per cent galactose, and 0.43 per cent sialic acid. Protein comprised 61.4–63.5 per cent of the total composition. Proline, glycine, and glutamic acid accounted for 65 per cent of the amino acid residues. Flatbed polyacrylamide electrophoresis revealed 17–18 bands. Immunoelectrophoresis using anti-parotid saliva sera revealed at least 12 antigens. Six of these were reactive with an anti-submaxillary saliva serum, while three were reactive with an anti-human serum. Fractionation of parotid saliva by DEAE-cellulose chromatography, separated the parotid antigens into reaction mixtures, which gave less complex patterns when examined by immunoelectrophoresis. Only one additional antigen was revealed that was not detected in the unfractionated secretion. The precipitin arcs of amylase, IgA, albumin, and a parotid glycoprotein were identified. Three other uncharacterized antigens were shown to share antigenic determinants with the parotid glycoprotein. The major advantage of immuno-electrophoresis was its ability to differentiate antigenically related components in complex mixtures.     

The composition of stimulated human parotid saliva

Isolated parotid saliva was collected from young, healthy volunteers first in the resting state, followed by stimulation with citric acid. Secretion rate, concentration of sodium, potassium, inorganic phosphate and protein as well as the activity of amylase and acid phosphatase were estimated. In response to stimulation, the secretion rate and sodium concentration of the saliva significantly increased and the concentration of inorganic phosphate and the activity of acid phosphatase significantly decreased. The mean value of potassium and protein concentration and amylase activity did not alter.Positive significant correlations were found between the unstimulated and stimulated saliva for potassium, phosphate and protein concentration and amylase activity. Comparing the secretion of the right and left gland positive, highly significant correlations were found for flow rate, potassium, phosphate and protein concentration and amylase activity. The diagnostic importance of these correlations are discussed.     

The composition of unstimulated human parotid saliva

Parotid saliva was collected separately in healthy volunteers and was analysed for sodium, potassium, phosphate and total protein concentration as well as for the activities of acid phosphatase and amylase. Simultaneous examination of the left and right parotid saliva revealed positive, highly significant correlations between the two sides in respect of secretion rate, potassium, phosphate and protein concentration and amylase activity. The diagnostic importance of these correlations is discussed.     

Purification and some properties of fucosyltransferase in human parotid saliva

Fucosyltransferase was purified from human parotid saliva by affinity chromatography on GDP-hexanolamine Sepharose, followed by chromatofocusing on PBE 94 exchanger gel. The purified enzyme had the N-acetyglucosaminide alpha 1----4, the N-acetylglucosaminide alpha 1----3, and the glucoside alpha 1----3 fucosyltransferase activities. The molecular weight of the purified enzyme was estimated to be approximately 20,000. These enzyme activities showed identical pH and divalent metal ion dependencies and identical rates of inactivation upon being heated. The paper chromatographic analysis of the fucosylated products by the purified enzyme and the susceptibility of these products to linkage-specific fucosidase digestion indicated that the transferase formed the Fuc alpha 1----4GlcNAc, Fuc alpha 1----3GlcNAc, and Fuc alpha 1----3Glc linkages.     

Heterogeneity of exo-type of beta-N-acetylglucosaminidase in human parotid saliva

The exo-type of β-N-acetylglucosaminidase (NAGase) in human parotid saliva was separated into two fractions, NAGase A and B, by diethylaminoethanol (DEAE)-cellulose column chromatography. The heterogeneity was confirmed by isoelectric focusing and disc electrophoresis. Isoelectric points of NAGase A and B were at pH 7.2 and 5.0, respectively. NAGase A was more heat-stable than NAGase B. A slight difference in pH optimum was found between NAGase A and B. Both components had almost the same Km values for p-nitrophenyl N-acetylβ-glucosaminide, p-nitrophenyl N-acetyl-β-galactosaminide, phenyl N-acetyl-β-glucosaminide and phenyl N-acetyl-β-galactosaminide.     

Characterization of the antioxidant profile of human saliva in peri-implant health and disease

OBJECTIVES: Peri-implant disease is considered to be an inflammatory disease, but many aspects of its pathogenesis remain unknown. At present, peri-implant disease is considered to be initiated and perpetuated by a small group of predominantly Gram-negative, anaerobic, or micro-aerophilic bacteria that colonize the subgingival area. Bacteria cause the observed tissue destruction directly by toxic products and indirectly by activating host defence systems, i.e. inflammation. A variety of molecular species appears in the inflamed tissues, among them are reactive species such as free radicals and reactive oxygen species (ROS). The purpose of this study was to assess levels of various antioxidants in saliva to identify differences between the saliva of patients with healthy peri-implant tissues and patients with peri-implant disease, and to examine whether the whole saliva of those with peri-implant disease conditions might have lower levels of antioxidants than that of healthy individuals. MATERIALS AND METHODS: Thirty healthy adult volunteers (14 men and 16 women) with implant-supported overdentures (Ankylos Biofunctional Implants) were selected from the group of patients from Tallinn Dental Clinic. Biochemical and clinical parameters evaluated were the following ones: the levels of urate, ascorbate, myeloperoxidase in saliva, total antioxidant status of saliva, pocket probing depth (mm), gingival index (0, 1, 2, or 3), and bleeding on probing (0 or 1). RESULTS AND CONCLUSION: Total antioxidant status (TAS) of saliva and concentration of uric acid and ascorbate, which are the main salivary antioxidants, are significantly decreased in patients with peri-implant disease. TAS in healthy subjects was 0.41+/-0.10 for resting saliva and 0.31+/-0.09 for stimulated saliva; in diseased subjects TAS was 0.19+/-0.07 and 0.12+/-0.03, respectively. In healthy subjects, the concentration of urate was 307.2+/-78.06 microM/l in resting saliva and 241.5+/-89.09 microM/l in stimulated saliva. In diseased patients, the concentration of urate was 120+/-36.13 and 91.60+/-39.35 microM/l, respectively. The concentration of ascorbate did not differ in resting and stimulated saliva. In healthy subjects, it was 2.79+/-0.81 mg/l and in diseased subjects, it was 1.54+/-0.30 mg/l. This may indicate that excessive ROS production in peri-implant disease is leading to the situation of excessive oxidative stress, which may be an important factor contributing the destruction of peri-implant tissues. The importance of these findings may be the better understanding of the processes involved in the pathogenesis of peri-implant disease and that the treatment of peri-implant disease may involve adjuvant anti-oxidants supplementation together with cumulative interceptive supportive therapy concept introduced by Mombelli & Lang.     

Immunoelectrophoretic identification of peroxidase in human parotid saliva.

Parotid saliva peroxidase was detected and identified in parotid saliva immunoelectropheretograms by heterologous cross-reacting antibodies to bovine lactoperoxidase and homologous antibodies to parotid saliva. The enzyme was moderately basic and located slightly cathodal to amylase at pH 7.2. Confirmation of identity of the precipitates was by specific enzymic disclosing reagents of the peroxidase-antibody complexes directly on the immunoelectropheretogram. Locating and identifying the peroxidase precipitin arc in the normal parotid saliva immunoelectropheretogram provides a means of detecting and studying pathological changes of the enzyme in parotid saliva.