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Uridine 5'-diphospho (UDP)-galactose: Nacetylglucosamine galactosyltransferase was separated from human parotid saliva and partially purified. The optimum pH of the enzyme was 7.5. The enzyme required a specific acceptor, and its activity was activated by manganese and magnesium ions. [ABSTRACT FROM AUTHOR]

Beta-N-acetylglucosaminidase in human parotid saliva was separated into two subfractions by diethylaminoethanol cellulose column chromatography. One subtraction of the enzyme was isolated and purified. Disk electrophoresis showed that the purified enzyme was homogeneous. The molecular weight of this enzyme was estimated to be about 153,000 by gel filtration and dodecyl sulfate polyacrylamide gel electrophoresis. N-acetyl-β-galactosaminides also were hydrolyzed by this enzyme at the same site. [ABSTRACT FROM AUTHOR]

Purified acid phosphomonoesterase from human parotid saliva has been characterized as an acid nucleotidase of broad specificity. The enzyme exhibited a pH optimum at 5.8 with 5'-AMP and was not metal dependent. Activity was inhibited greatly by mercuric ions, sodium fluoride, and sodium tartrate. The tartrate inhibition was competitive. [ABSTRACT FROM AUTHOR]

Lysozyme from human parotid saliva was purified to the point where it was judged, by the criteria of ultracentrifugation and disk electrophoresis, to be homogeneous. The parotid lysozyme had a specific activity 3.5 times greater than that of hen egg-white lysozyme and a composition that was different, especially in regard to tyrosine, serine, and glutamic acid content. The molecular weight was determined to be around 14,300. When tryptophan residues were modified with N-bromosuccinamide, no lytic activity was found, which indicates that the tryptophan residues may play an important role in the maintenance of the parotid lysozyme activity. [ABSTRACT FROM AUTHOR]

Acid phosphomonoesterase was separated from human parotid saliva and purified. The purified enzyme was proved homogeneous on sedimentation and disk electrophoresis. The optimal pH of the enzyme was 3.3. The enzyme had no substrate specificity for phosphomonoesters and its activity was inhibited by SnF2 or NaF. [ABSTRACT FROM AUTHOR]

This article reports on glycoprotein in parotid saliva and oral streptococci. Salivary constituents such as antibodies, lysozyme, and various aggregating factors interact with oral bacteria such as Streptococcus sanguis and Streptococcus mutans. The article also discusses salivary-bacterial interactions in terms of purified glycoproteins, proline, and binding. Information is also provided on streptococcal cultures and strains, incubation, and centrifugation before radioactive testing. A table of binding results is presented as well.