Cyclopolymerisation. 3. Mitt. ESR-Untersuchungen von Diallylaminen mit Redox-Systemen

Ohne Zusammenfassung     

Covalent bonding of alkene and alkyne reagents to graphitic carbon surfaces

Various aromatic and aliphatic alkynes and one alkene were covalently bonded to sp(2)-hybridized carbon surfaces by heat treatment in an argon atmosphere. X-ray photoelectron spectroscopy, Raman, and FTIR spectra of the modified surfaces showed that the molecules were intact after the 400 degrees C heat treatment but that the alkyne group had reacted with the surface to form a covalent bond. Alkynes with ferrocene and porphyrin centers exhibited chemically reversible voltammetric waves that could be cycled many times. Atomic force microscopy of the modified surfaces indicated a thickness of the molecular layer consistent with monolayer coverage, and surface coverage determined by voltammetry was also in the monolayer range. Raman spectroscopy of the porphyrin monolayers formed from a porphyrin alkyne showed no evidence for dimer formation, although multilayer formation may occur at undetected levels. FTIR spectra of the porphyrin-modified carbon surfaces were well-defined, similar to the parent molecule, and indicative of an average tilt angle between the porphyrin plane and the surface normal of 37 degrees . The bond between the molecular monolayer and the carbon surface was quite stable, withstanding sonication in tetrahydrofuran, mild aqueous acid and base, and repeated voltammetric cycling in propylene carbonate electrolyte. Heat treatment of alkynes and alkenes appears to be a generally useful method for modifying carbon surfaces, which can be applied to both aromatic and aliphatic molecules.     

Anisotropic membranes with carboxypeptidase G1

Anisotropic polysulfone membranes were prepared with carboxypeptidase G₁ embedded in the polymer structure. The enzymatically active flat and hollow-fiber membranes were obtained by precipitating the polymer from solution in an organic mixture in which an aqueous solution of the enzyme had been dispersed. The process has been found to be particularly suitable for the immobilization of enzymes in anisotropic hollow fibers that exhibited no detectable enzyme leakage upon perfusion. The pH profiles measured with the enzyme in free solution and in the embedded form were similar. Kinetic parameters of multitubular enzyme reactors were investigated by measuring the rate of hydrolysis of glutamate from folic acid or methotrexate at different flow rates and substrate concentrations. The relatively slow mass transfer in such reactors was found to affect strongly the observed kinetics. The results of in vitro experiments with 5000 fiber reactors suggest that hollow fiber cartridges prepared with such membranes have clinical potential for the extracorporeal removal of methotrexate from blood.     

Oxygen binding of water-soluble cobalt porphyrins in aqueous solution

Water-soluble cobalt porphyrin 1Co and imidazole ligand 2 were synthesized. 1Co binds dioxygen in the presence of imidazole ligand 2 in aqueous solution. The formation of the oxygen adduct 2-1Co(O(2)) was studied using UV-vis and EPR spectroscopy. The impact of pH on the kinetic stability of the oxygen adduct was examined.     

Flavin-protein interaction in bound glucose oxidase

Glucose oxidase was bound to Sepharose, Sephadex, gelatin, and dextran, yielding immobilized soluble and insoluble derivatives of the enzyme. The soluble preparations possessed higher enzymic activity than the analogous insoluble ones. The reversible dissociation process of the bound enzyme into apoenzyme and flavin adenine dinucleotide (FAD) was studied with the soluble and insoluble glucose oxidase in relation to enzymic activity and conformational changes as measured by circular dichroism and fluorescence methods. Bound apoenzyme was found to be more stable than the apoenzyme obtained from the unmodified glucose oxidase. The binding constant of FAD in bound glucose oxidase (K_diss≈10^-8M) calculated from fluorescent studies was lower than that of FAD in the native enzyme (K_diss10^-10M). The circular dichroism measurements indicated that dextran-bound glucose oxidase has a conformation similar to that of the native enzyme.