Effect of retinoic acid on the aggregation of erythrocytes and leukocytes in the blood

Human and animal blood smear staining with PAPh has revealed mononuclear leukocyte-erythrocyte aggregates. Administration of retinoic acid increased concentration and dimensions of these aggregates and was followed by preferential accumulation of PAPh-negative osmotically unstable erythrocytes. Similar changes were detected in the blood samples of women engaged in the production of retinoic acid. Aggregate concentration showed positive correlation with erythrocyte sedimentation rate and no correlation with prothrombin time.     

Fatty acid composition of Escherichia coli cells and their viability in air

Experiments on E. coli used as a model have revealed that fatty-acid composition is one of the characteristics which determine the viability of bacteria in the air. The viability of microbial cells in the air has been shown to increase with the increase of the pool of cyclopropane acids and the palmitic acid/palmitoleic acid ratio in the cells, irrespective of their genotype and the phase of their growth.     

Hexameric purine nucleoside phosphorylase II from Escherichia coli K-12. Physico-chemical and catalytic properties and stabilization with substrates

Some properties of hexameric purine nucleoside phosphorylase II (EC 2.4.2.1) from Escherichia coli K-12 were studied. The enzyme obeys the Michaelis-Menten kinetics with respect to purine substrates (Km for inosine, deoxyinosine and hypoxanthine are equal to 492, 106 and 26.6 microM, respectively) and exhibits negative kinetic cooperativity towards phosphate and ribose-1-phosphate. The Hill coefficient is equal to approximately 0.5 for both substrates. Hexameric purine nucleoside phosphorylase II is not a metal-dependent enzyme; its activity is inhibited by Cu2+, Zn2+, Ni2+ and SO4(2-). The enzyme is the most stable at pH 6.0; it contains essential thiol groups. All substrates partly protect the enzyme against inactivation by 5.5'-dithiobis(2-nitrobenzoic acid) and heat-inactivation and, with the exception of phosphate-against inactivation by p-chloromercuribenzoate. Hypoxanthine, especially in combination with phosphate, afford the best protection against inactivation.     

Liver mitochondria, confirmed as intact by complete suppression of succinate uptake and oxidation, possess a carnitine palmitoyltransferase I that is totally inhibited by malonyl CoA.

Succinate dehydrogenase activity in mitochondria, which were isolated by centrifuging partially purified mitochondria through 1. 315 M sucrose, was completely suppressed when [14C]succinate uptake was abolished by prior incubation of the mitochondria with carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) and valinomycin. The conclusion that these mitochondria were intact was confirmed by the fact that, when these mitochondria were broken by a freeze-thaw cycle followed by sonication, such inhibition was totally abolished. The yield of mitochondria, microsomes, and peroxisomes from the initial homogenate was 17.8, <0.1, and 0%, respectively, indicating that the mitochondria were not only intact but also essentially free of contamination from microsomes and peroxisomes. The overt form of carnitine palmitoyltransferase (CPT I) in these intact and pure mitochondria was totally inhibited by malonyl CoA, indicating that previous reports of incomplete inhibition in mitochondrial preparations resulted from interference from CPT activity in the inner mitochondrial membrane (CPT II), microsomes, or peroxisomes.     

Die Wuchsstoffleitung in der Pflanze I

Zusammenfassung In Blättern vonColeus-rot und in Kotyledonen vonCucumis sativa wird künstlich durch die Epidermis zugeführter Wuchsstoff (Heteroauxin) apikalwärts geleitet, wenn der direkte Abfluß nach der Mittelrippe unterbunden ist. Daraus folgt, daß die Wuchsstoffleitung in der Pflanze keine streng polare Erscheinung ist, genau so wenig, wie der Transpirationsstrom oder der Strom der Assimilate streng polar fließen.Mit 11 Textabbildungen (16 Einzelbildern).Mit Unterstützung der Deutschen Forschungsgemeinschaft und der William G. Kerckhoff-Stiftung zu Bad Nauheim.