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R Reissbrodt

Publications and source records attributed to R Reissbrodt.

67 records · Page 4Linked to original sources
PubMed1978

[The localization of the anodically-moving thermolabile antigen (ATA) of gram-negative bacteria with ferritin-labelled antibodies (author's transl)].

In studies on the antigenic structure of shigellae, an anodically-moving thermolabile antigen (ATA) was found, which furthermore could be detected in many other enterobacteriae (9, 10). ATA is a glycoprotein with a high molecular heterogeneity, resulting from aggregates of a subunit with a molecular weight of about 22000 Daltons. In the present paper the antigen was localized on the cell surface of several species by means of the immunoferritin technique. Antibodies against the purified ATA were raised in rabbits and were coupled with ferritin using glutaraldehyde. The antigen was found focally distributed over the whole circumference of the cell. According to the location of the ferritin granules, the ATA is tightly attached to the outer membrane. Especially some rough forms of the bacteria were heavily labelled on their surface. From the results obtained we conclude that in the smooth form the polysaccharide side chains of the somatic antigen cover the ATA.

Antibodies, Bacterial↗
PubMed1976

[The anodically moving thermolabile antigen (ATA) of gram-negative bacteria: its molecular heterogeneity and its chemical composition].

The anodically-moving thermolabile antigen (ATA) of gram-negative bacteria represents a glycolipoprote in. In aqueous solution ATA exhibits heterogeneity of the molecular size, the range varying between 2.10(4) and 8.10(5) Daltons. In the molecular range between 5.10(4) and 8.10(5) all the molecular states give precipitation lines with the corresponding antisera. It could be shown that all the molecular states of ATA are formed by different aggregation of the same subunit with a molecular weight of approximatively 22000.

Amino Acids↗
PubMed1975

[The anodic-moving thermolabile antigen (ATA) of gram-negative bacteria: its occurrence in rough mutants of shigella flexneri and Escherichia coli(author's transl)].

The thermolabile antigen (ATA) moving to the anode, discovered by us (9) and also described by LARSSON et al. (8), could be detected in Ra-, Rb-, Re- and Rd-mutants of Sh. flexneri and, in smaller amounts, in Rd- and Re- mutants of E. coli O8:K27:H. So it proves to be different from KUNIN'S common antigen (7). Our results lead to the conclusion that ATA is located in a more inner part of the bacterial cell wall and is fixed by noncovalent linkages.

Antigens, Bacterial↗
PubMed1975

[Dependence of various antigen formation of Proteus mirabilis strain 1095/67 growing on minimal nutrient media].

Proteus mirabilis strain 1095/67 has been cultivated in surface culture on different minimal media, which were composed either of single amino acids or combinations of several amino acids without or with stepwise addition of other C-sources up to the complete medium. We found a direct dependence of the formation of the various antigens (moving to the cathode, to the anode, or not moving) on the composition of the medium. Certain amino acids (Ala, Glu, Asp. Ser) elicit only parts of the antigenic spectrum formed in complete medium, but enrich special antigens. With only 2 amino acids (Ala and Glu) and the vitamins thiamine, pyridoxal, and niacine in the anorganic basic medium the complete antigenic spectrum can be formed. We have shown that the composition of the cell wall varies with the composition of the culture medium. In shaked cultures we found serine to be essential for the production of the antigen moving to the cathode and the thermolabile antigene moving to the anode (ATA), niacine to be of fundamental importance in the biosynthesis of all antigens. Already under very limited supply of nutrients ATA, common to all gram-negative bacteria, is formed and, therefore, it seems to be a very basic cell wall component.

Amino Acids↗
PubMedDate not supplied

Computer-aided design of novel siderophores: pyridinochelin.

Pyridinochelin, a novel tetradentate catecholate-type siderophore, has been designed on the basis of the active analog enterobactin and was then synthesized. Growth promotion tests indicate that this synthetic siderophore feeds various pathogenic bacteria most effectively with iron even though it lacks one catecholate group compared to enterobactin. The superposition of the mentioned siderophore structures suggests that the structure of the skeleton connecting the catecholate groups might be an important factor for the iron transport.

Bacteria↗