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G J Revis

Publications and source records attributed to G J Revis.

6 recordsLinked to original sources

Identification of transcalciferin as a major component of human parotid saliva by crossed immunoelectrophoretic mapping.

Human parotid saliva collected from Stenson's duct during sour candy-stimulated salivation was studied by crossed immunoelectrophoresis (X-IEP). Eleven antigens were identified in a pool of salivas from 10 adult, caucasoid males and females. Four were related to serum antigens, three being previously known: IgG, IgA and albumin. The fourth was identified as Gc globulin, also known by function as transcalciferin. Salivary Gc is electrophoretically different from serum Gc, migrating as an alpha 2-beta component rather than as an alpha 1 globulin. The quantities of 8 of the 11 antigens detected by X-IEP were compared for salivas from 10 subjects. These quantities and their ratios to each other were highly variable, indicating idiosyncratic secretory patterns. Only quantities of amylase were moderately consistent from donor to donor. Quantitatively, Gc is a major antigen in parotid saliva. Large proportions of a salivary antigen, alpha 1c, were found in two of the 10 subjects--adult males who never had developed caries. Among the other 8 subjects, all with caries, proportions of alpha 1c were much lower, and 2 subjects lacked it. None of the other antigens measured showed any correlation with caries resistance. The nature and function of alpha 1c are unknown.

Adult↗

Antibodies against the Ag2 fimbriae of Actinomyces viscosus T14V inhibit lactose-sensitive bacterial adherence.

Monospecific antisera against the Ag1 and Ag2 fimbrial components of Actinomyces viscosus T14V were produced by immunizing rabbits with immune precipitates of each antigen harvested from crossed-immunoelectrophoresis plates. The Fab fragments prepared from these sera were used as specific reagents in immunoelectron microscopy to identify each fimbrial component on the bacterial surface and also were assayed for their abilities to prevent the coaggregation of A. viscosus T14V with Streptococcus sanguis 34, an interaction that is lactose sensitive. Each Fab preparation appeared to react with different fibrillar structures present on the actinomycete, and only the Ag2-specific Fabs blocked coaggregation. These results provide strong support for the presence of distinct types of fimbriae on A. viscosus T14V and indicate the exclusive involvement of Ag2 fimbriae in lactose-sensitive adherence.

Actinomyces↗