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Biomedical subjects

A Grov

Publications and source records attributed to A Grov.

At least 37 records · Page 2Linked to original sources
PubMed1976

The effect of specific antibodies on the inhibition of leucocyte migration caused by staphylococcal peptidoglycan.

Specific antibodies to the various antigenic determinants of staphylococcal peptidoglycan are tested for neutralization of the inhibiting effect of peptidoglycan on leucocyte migration. Antibodies to the C-terminal D-Ala-D-Ala group of pentapeptides and to the C-terminal of the glycine bridge showed high neutralizing effect, whereas that of antibodies to the tetrapeptide and to the glycan chain was negligible. The observed neutralization of antibodies against the outermost parts of peptide chains may be due to the inhibition of contact between peptidoglycan and cells.

Antibodies, Bacterial↗
PubMed1976

Human colostral IgA interacting with staphylococcal protein A.

Human colostral IgA from three apparently healthy mothers were all divided into protein A reactive and protein A non-reactive fractions on a Sepharose-protein A column. The reactive fractions, giving no direct precipitation but co-precipitations, were found to interact with protein A through the Fc-region.

Bacterial Proteins↗
PubMed1975

Localization of antigens in thin sections of bacteria by the immuno-peroxidase technique.

The immunoperoxidase technique together with electron microscopy has been examined for the ultrastructural localization of staphylococcal protein A, the immunoferritin method being included for comparison. The results show that protein A is uniformly distributed in the whole cell wall. Both the direct and indirect methods, Fab- as well as Fc-reactions, showed identical results. tthe immunoperoxidase method was superior to the immunoferritin method, especially when applied to thin sections of the bacteria, and the clear specificity demonstrated indicates a useful method for localization of cellular antigens.

Animals↗
PubMed1975

Studies on polysaccharide C of Staphylococcus epidermidis. 1. Isolation and chemical characterization.

Polysaccharide C (poly C) has been isolated from two strains of S. epidermidis and characterized chemically. The results suggest that poly C is a wall N-acetylglucosaminylglycerol teichoic acid, linked through 1:3-phosphodiester linkages. One poly C preparation contained only beta-linked N-acetyglucosamine, the other traces of alpha-linked sugar in addition. The degree of substitution of sugar in the poly C preparations from the two strains was about 50 and 25 per cent.

Acetylglucosamine↗
PubMed1975

Studies on polysaccharide C of staphylococcus epidermidis. 2. Antigenic properties.

The antigenic properties of polysaccharide C (poly C) of S. epidermidis strongly support the analytical indications that it is an N-acetylglucosaminylglycerol teichoic acid with 1:3-phosphodiester linkages. The major antigenic determinant is N-acetyglucosamine, predominantly present in the beta-configuration. Also anti-glycerophosphate antibodies are produced, apparently dependent on the degree of glycosylation. Purified poly C was unable to sensitize either normal or tanned sheep erythrocytes for agglutination in antisera.

Acetylglucosamine↗
PubMed1975

Estimation of peptidoglycan antibodies by an immunoperoxidase technique.

An immunoperoxidase technique developed for the detection and measurement of anti-peptidoglycan antibodies is described. The technique is based on the Mancini single radial immunodiffusion test with the addition of a reaction step with peroxidase-labelled anti-immunoglobulins. The dark-brown colour produced by the enzyme and a H2O2-diaminobenzidine solution increased the sensitivity considerably. The test was found to be highly specific and valuable both for the screening of total amounts of anti-peptidoglycan antibodies in sera as well as in studies of antibody specificity.

3,3'-Diaminobenzidine↗