An extended kinetic analysis of valinomycin-induced Rb-transport through monoglyceride membranes.

The time course of the current following a voltage jump, which is applied to monoglyceride bilayers in the presence of valinomycin, shows two relaxation times. This is basically in agreement with a simple carrier model which has been described in full detail formerly. Relaxation times and amplitudes allow a calculation of the rate constants of the transport model. The presented data supplement an analysis which was hitherto based only on the slower relaxation process and on information derived from the nonlinearity of current-voltage characteristics. The additional resolution of the faster relaxation time allowed an approximate determination of the voltage dependence of the translocation rate constant for carrier-ion-complex and provided evidence for a small voltage dependence of the interfacial reaction. The dependence of the relaxation parameters on the ion concentration in the aqueous phase was interpreted assuming a saturation of the ion concentration at the reaction plane at high bulk concentrations.     

Allylic palladium(II) triazenido complexes: synthesis and spectroscopic studies

Reaction of [Pd(1-3-η-allyl)Cl]₂ with lithium triazenide (triazenide = p-XC₆H₄NN-NC₆H₄X-p; X = Cl, H, CH₃) affords dimeric complexes of the type [Pd(1-3-η-allyl)(triazenide)]₂. In the solid state the triazenido ligands are bridging two palladium atoms with their terminal nitrogen atoms, as shown by a preliminary X-ray determination of the complex with X = CH₃. The allyl groups are stereochemically equivalent. ¹H NMR spectra demonstrate the presence of two conformers in solution. The major component has the same configuration found in the solid. The other conformer has stereochemically non equivalent allyl groups. The concentration ratio of the two conformers is independent of the temperature, suggesting the absence of intramolecular processes and of palladium- triazenido bond breaking. This point is discussed also by comparing the (1-3-η-allyl)(triazenide)palladium (II) dimers with the closely related(1-3-η-allyl)(acetate)palladium(II) complexes.     

Acetylene reduction by nitrogen-fixing blue-green algae

Summary Known nitrogen-fixing species of blue-green algae are capable of reducing acetylene to ethylene, but acetylene is not reduced by Anacystis nidulans, which does not fix nitrogen. Cycad root nodules which contain blue-green algae as endophytes reduce acetylene. Acetylene reduction is inhibited by carbon monoxide. Nitrate or ammonium-nitrogen has no immediate effect on algae reducing acetylene, but algae grown on nitrate-nitrogen gradually lose their capacity to reduce acetylene. Nitrate-nitrogen also inhibits heterocyst formation in these algae and there is a fairly direct correlation between the abundance of heterocysts in a particular sample and its capacity to reduce acetylene. Aphanizomenon flosaquae reduces acetylene and fixes nitrogen in unialgal culture and there is strong presumptive evidence that these reductions are carried out by the alga rather than by associated bacteria. The molar ratios of ethylene: ammonia produced vary within the range 1.4–1.8.     

The existence of a second route for the transfer of certain glycoproteins from the circulation into the liver.

Oligosaccharide chains of agalactoorosomucoid, α₁-acid glycoprotein from which sialic acid and galactose have been sequentially removed, terminate in N-acetylglucosaminyl residues. This protein is rapidly transferred from the circulation into the liver by a route distinct from that previously demonstrated for a number of galactosyl terminating glycoproteins.     

Purification of prostaglandin E2-9-oxoreductase from human decidua vera

Prostaglandin E2-9- oxoreductase (PGE2-9-OR), the enzyme which converts prostaglandin E2 (PGE2) to prostaglandin F2 alpha (PGF2 alpha), has been detected in human decidua vera. A 105-fold purification was achieved when the centrifuged homogenate was fractionated sequentially by DEAE-Trisacryl, hydroxyapatite-agarose gel, ultrogel AcA 44 and Matrex gel blue A gel chromatographies. The following kinetic constants for PGE2-9-OR have been obtained. The equilibrium constant with respect to PGE2 is 83 microM, the Michaelis constant, Km, for PGE2 is 80 microM, for NADPH 1.6 microM. The maximal velocity for the forward reaction is V1 = .203 pmol/min. The enzyme was inhibited by progesterone, oestradiol-17 beta, cortisol and pharmaceutical drugs. An activating effect could be demonstrated with Ca2+ and oxytocin. The occurrence of PGE2-9-OR in the decidua vera suggests that this enzyme may be responsible for the transformation of PGE2 to PGF2 alpha in these tissues. This may be an important mechanism for the initiation and maintenance of uterine contractions.