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Biomedical subjects

F M Eggert

Publications and source records attributed to F M Eggert.

25 records · Page 2Linked to original sources
PubMed1980

The nature of secretory agglutinins and aggregating factors. IV. Complexing between non-mucin glycoproteins, immunoglobulins and mucins in human saliva and amniotic fluid.

By themselves the non-mucin glycoproteins of saliva and amniotic fluid produce secretory conglutinin-like factor (SKF) and secretory bacterial aggregating factor (SBAF) activity. These glycoproteins also bind immunoglobulins; a secretory binding factor for immunoglobulins (SBFI) with EDTA-reversible activity is found in amniotic fluid. Agglutination of particles by very small amounts of secretory antibody is facilitated by reversible and irreversible binding of antibody to SKF/SBAF active glycoproteins. EDTA effects on the carrier glycoproteins make the bound antibody activity EDTA-sensitive. The SKF/SBAF glycoproteins also have EDTA-sensitive interactions with each other and possibly with mucins. These complex interactions of secretory glycoproteins and immunoglobulins are of importance in mucosal protection.

Agglutinins↗
PubMed1979

Rapid demineralization in acidic buffers.

The demineralization of routine histological specimens in buffers of weakly ionized organic acids, unbuffered formic acid, and EDTA was investigated. The rate of demineralization was measured by a chemical method and from radiographs. Lactate-containing buffers and buffers of formic acid with its potassium salt were more rapid in effect than any other agent. Acidic buffers and unbuffered formic acid produced rapid diffuse demineralization with secondary precipitation of calcium salts. Preservation of dental enamel in such buffers resulted from the significantly slower rate of enamel demineralization than that for bone and dentine. In rapid demineralizing agents the secondary salts were quickly redissolved while in slow buffers these salts persisted. Multivalent ions such as citrate and maleate slowed the rate of demineralization, and a citrate-containing buffer was the slowest of all the agents tested. Demineralization in EDTA exhibited a different pattern with the establishment of a well-defined front of demineralization without apparent reprecipitation. EDTA attacked enamel, bone and dentine at the same rate. An attempt was made to relate the observed rates of demineralization to current theories of the demineralization process.

Animals↗
PubMed1979

A simplified procedure for measuring the class of anti-bacterial antibodies by mixed reverse passive antiglobulin haemagglutination (MRPAH).

A modified procedure is described for performing the MRPAH (mixed reverse passive antiglobulin haemagglutination) reaction as a simple micro-method to measure the classes of bacterial antibodies. This 'bacterial dilution procedure' gave results closely correlated with those obtained by the 'serum (sample) dilution procedure' previously reported and with great economy of materials, labour and time. The method was used to investigate human serum antibodies to Br. abortus and S. enteritidis and serum and secretory antibodies to Strep. mutans. The good reproducibility of the MRPAH reaction was demonstrated by re-examining brucellosis sera tested one year previously. MRPAH was sufficiently sensitive to demonstrate the small amounts of IgG and IgM antibodies to Strep. mutans in human colostrum and early milk. A rise of antibody levels in the different immunoglobulin classes G, A and M was readily demonstrated in sera from individuals with salmonellosis.

Animals↗
PubMed1973

Amelogenins. Purification and partial characterization of proteins from developing bovine dental enamel.

1. Procedures are described for the purification of amelogenin electrophoretic components and their analysis for homogeneity by polyacrylamide-gel electrophoresis at both acidic and alkaline pH values. 2. Most of these components belonged to two main groups, termed the J group and the C group after their major electrophoretic components. Sodium dodecyl sulphate-polyacrylamide-gel electrophoresis indicated that, within each group, proteins were of similar size, but the C-group proteins were larger than those of the J group. 3. By sedimentation-equilibrium ultracentrifugation and amino acid analysis, the four J-group components were found to be very small proteins (mol. wt. 5500-3000) and, except for one, similar in amino acid composition. The components of the C group were found to be proteins of moderate size (mol. wt. 16800-16100) with very similar amino acid compositions. A third minor amelogenin group of intermediate size was also found, but not further analysed. Details of the results of the ultracentrifuge studies are given in a supplementary paper that has been deposited as Supplementary Publication SUP 50014 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5. 4. Two of the J-group components were similar to amelogenins isolated by other workers. 5. All amelogenins analysed were rich in proline, glutamic acid, histidine and methionine, and contained no half-cystine. Their amino acid compositions, combined with their molecular weights, serve to distinguish the amelogenins from both collagens and keratins.

Amelogenesis↗
PubMedDate not supplied

Antimicrobial resistance: dentistry's role.

The resistance of bacteria, fungi and viruses to antimicrobials is increasing rapidly, with deleterious consequences. Dentistry's role in this development is unclear, because the necessary information has not yet been collected. Nevertheless, dentists should recognize that it is essential to use antimicrobials in an appropriate and responsible manner, both to treat infection effectively, and to minimize the likelihood that the bacteria in the general population will develop resistance to antimicrobials. The purpose of this article is to make dentists aware of the concerns raised by antimicrobial resistance, and how it can be avoided.

Anti-Bacterial Agents↗