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Zusammenfassung Zn++, Mg++ und Mn++-Ionen stimulieren bei gewissen Konzentrationen den Einbau von C14-acetat in Aflatoxinen durch ruhende Mycelien desAspergillus parasitic in tris-HCl-Puffer bei pH 7,2. Ba++ gaben Aktivierungen über einen weiten Konzentrationsbereich, während Äthanol den Einbau verhindert. Von den Intermedärprodukten des 3-Carbonsäure-Cyclus gab die Citronensäure ein Maximum an Aktivierung.

Zusammenfassung Die Wirkung verschiedener Einflüsse wie pH-Wert, Puffer, Natriumchlorid und UV-Bestrahlung auf die Fluorescenz von Aflatoxin Bi und G1 wurde untersucht. Die Fluorescenzcharakteristik der Aflatoxine B1 und G1 unterliegt charakteristischen Veränderungen bei pH-Werten über 7,2. Verlängerte Bestrahlung mit UV führte zum Abbau der Aflatoxine, wobei die Intensität von der Natur des Lösungsmittels abhängig ist. Natriumchlorid schützte teilweise die Toxine vor dem Abbau durch UV oder in alkalischer Lösung.[/p]

Effect of excess feeding and depletion of vitamin A on the ability of adipose tissue to maintain plasma free fatty acid levels has been studied in rats. Both in hypervitaminosis A (fed 9 mg of retinol for 2 consecutive days) and in vitamin A deficiency (kept on a vitamin A-deficient diet for 6 weeks) the rats showed elevated levels of plasma free fatty acids. Hypervitaminosis A caused a decrease in the fatty acid release from adipose tissue on in vitroincubation, probably due to lowered levels of cyclic AMP. On the other hand, adipose tissue from vitamin A-deficient animals showed an increased lipolytic rate as compared to that of the controls. No change in the lipogenic ability was indicated in either of the conditions as indicated by the activities of enzymes involved in this process. We conclude that the fatty acid homeostasis can be greatly influenced by the vitamin A status of the animals.

Abstract: An aldolase was partially purified from fermenter grownMycobacterium tuberculosis H37Rv cells. The aldolase has a molecular weight of 150,000, possesses a tetrameric structure and cleaves both fructose diphosphate and fructose-1-phosphate, the former being cleaved 17 times faster. The enzyme was inactivated by treatment with NaBH4 in the presence of fructose diphosphate or dihydroxyacetone, phosphate suggesting Schiff base formation during its catalytic function. Thiol reagents, EDTA and metal ions had no apparent effect on the aldolase activity. These results show that aldolase is of Class I type. However, this enzyme, unlike the mammalian Class I aldolase, was unaffected by carboxypeptidase A. N-ethylmaleiniide and dithionitrobenzoic acid.

Summary The interaction of aflatoxin B1 with a number of biologically important substances has been investigated by spectrophotometric and fluorimetric techniques. The ultra-violet absorption of tryptophan, adenosine, RNA and DNA were altered by the addition of aflatoxin B1. Some amino-acids, purine and pyrimidine derivatives, bovine-serum albumin and DNA quenched the fluorescence of aflatoxin B1. Fluorescence polarization data suggested that the interaction of aflatoxin B1 with bovine-serum albumin was stronger than that with DNA.

The phospholipid-associated protein (55–67 kDa) fraction of Mycobacterium tuberculosis H37Rv was purified as the DE-V protein fraction. This DE-V fraction was used for diagnosis of tuberculosis by enzyme-linked immunosorbent assay (ELISA), detecting IgG antibody in sera collected from different categories of tuberculosis patients, i.e. with acid fast bacilli (AFB) culture-positive pulmonary tuberculosis, with AFB culture-negative, but radiologically suspected, pulmonary tuberculosis, extrapulmonary tuberculosis, and control groups of patients suffering from diseases other than tuberculosis (asthma and/or rhinitis, lepromatous leprosy) as well as from healthy volunteers. Encouraging operational ELISA validity could be achieved with 93% sensitivity, 100% specificity, 97% efficiency, 100% positive predictivity and 95% negative predictability even among the extrapulmonary and suspected pulmonary tuberculosis patients. The above assay was insensitive but with 100% specificity among control group of patients suffering from diseases other than tuberculosis. The DE-V protein fraction was associated with phosphatidyl inositol and phosphatidyl inositol mannosides. The dissociation of phospholipid-protein complex decreased ELISA specificity. ELISA reactivity of the DE-V fraction appeared to be thermostable; thus, it may have serodiagnostic utility in developing countries.

Uptake of radioactive tryptophan by Mycobacterium tuberculosisH37Rv grown in vitro and in vivo was investigated. Kmvalues indicated low affinity, and sodium azide inhibited uptake. Rifampin at the minimal inhibitory concentration had no effect, whereas ethambutol inhibited uptake only in the bacilli grown under in vitro conditions. The significance of these results is discussed.

1. Activation of glucose 6-phosphate is one of the unique properties of pyruvate kinase from Mycobacterium smegmatis. 2. Pyruvate kinase, partially purified from ultrasonic extracts of the mycobacteria by (NH4)2SO4 fractionation, exhibited sigmoidal kinetics at various concentrations of phosphoenolpyruvate, with a high degree of co-operativity (Hill coefficient, h = 3.7) and S0.5 value of 1.0 mM. 3. In the presence of glucose 6-phosphate, the degree of co-operativity shown by the phosphoenolpyruvate saturation curve was decreased to h = 2.33 and the S0.5 value was lowered to 0.47 mM. 4. The enzyme was activated by AMP and ribose 5-phosphate also, but the activation constant was lowest with glucose 6-phosphate (0.24 mM). 5. The enzyme was strongly inhibited by ATP at all phosphoenolpyruvate concentrations. The concentrations of ATP required to produce half-maximal inhibition of enzyme activity at non-saturating (0.2 mM) and saturating (2 mM) phosphoenolpyruvate concentrations were 1.1 mM and 3 mM respectively. 6. The inhibition of ATP was partially relieved by glucose 6-phosphate. 7. The enzyme exhibited Michaelis-Menten kinetics with ADP as the variable substrate, with an apparent Km of 0.66 mM. 8. The enzyme required Mg2+ or Mn2+ ions for activity. It was not activated by univalent cations. 9. The kinetic data indicate that under physiological conditions glucose 6-phosphate probably plays a significant role in the regulation of pyruvate kinase activity.

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Copyright of Zeitschrift für Lebensmittel-Untersuchung und -Forschung is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Zeitschrift für Lebensmittel-Untersuchung und -Forschung is the property of Springer Nature and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)