Folia Microbiologica

Janecek, J.; Rickenberg, H. V.

doi: 10.1007/bf02872693pmid: 4897960

Glucose and its close metabolic derivatives were compared for their effectiveness in bringing about catabolite repression inEscherichia coli. The findings indicate that catabolite repression is established most rapidly when glucose-6-phosphate serves as source of carbon; they also demonstrate that regulation by catabolite repression is exerted at the level of transcription.

Moses, V.; Wild, D. G.

doi: 10.1007/bf02872696pmid: 4897961

Bergter, F.; Knöll, H.; Noack, D.

doi: 10.1007/bf02872697pmid: 4897962

Kamarytová, V.

doi: 10.1007/bf02872702pmid: 4185979

The number of cells containing gammaglobulin in the regional lymphatic nodes of rabbits during the response to the single local dose of diphtheria toxoid was demonstrated using immunofluorescent technique. Antigen-dependent increase of the number of IgG—containing cells in regional lymph nodes was found. The possible source of the gammaglobulin without demonstrable specificity to the administered antigen is discussed.

Voříšek, J.; Powell, A. J.; Vaněk, Z.

doi: 10.1007/bf02872709pmid: 5820752

The activity of PEP carboxylase (E.C.4.1.1.31) was demonstrated in cell free extracts ofStreptomyces aureofacines. The enzyme was purified 610 fold. AcetylCoA increased the affinity of the purified enzyme for substrate approximately tenfold and doubled the specific activity of the enzyme preparation. Inorganic phosphate was not essential for the reaction; on the contrary, it had an inhibitory effect. Essential cofactors were divalent cations, the most potent of which was Mn2+. The kinetic characters of the purified enzyme were similar to figures for PEP carboxylase from other sources. The substrate saturation function replotted according to the Hill equation showed the extent of intramolecular interactions, reflecting the allosteric nature of the enzyme.