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Biomedical subjects

K Mosbach

Publications and source records attributed to K Mosbach.

At least 217 records · Page 12Linked to original sources

Coconut and Salmonella infection.

Raw, unprocessed coconut supports the growth of salmonellae as well as that of other enteric bacteria, salmonellae being particularly resistant to subsequent desiccation. Original contamination is not due to carriers or to polluted water supplies, but to contact with bacteria-containing soils followed by dispersion via infected coconut milk and shells. Pasteurization of raw coconut meat in a water bath at 80 C for 8 to 10 min effectively killed such bacteria, did not injure the product, and provided a prophylactic method now widely used by the coconut industry.

Cocos↗

Some recent developments in the preparation of novel recognition systems: a recognition site for the selective catalysis of an aldol condensation using molecular imprinting and specific affinity motifs for alpha-chymotrypsin using a phage display peptide library.

Molecular imprinting and phage display library technologies are rapidly being accepted as useful techniques for the generation of ligand-selective recognition motifs. The use of molecular imprinting to produce a novel type II aldolase mimic selective for the cobalt(II)-mediated aldol condensation of benzophenone and acetaldehyde is reported here. Furthermore, peptide motifs have been identified which are acting as 'affinity ligands' selective for the recognition of the enzyme alpha-chymotrypsin using phage display techniques.

Acetaldehyde↗

Study of the nature of recognition in molecularly imprinted polymers.

In the present study molecularly imprinted polymers (MIPs) were prepared against a series of structurally related compounds containing various numbers of pyridyl groups. The goal, to increase understanding of the mechanisms of recognition in MIPs, was achieved by comparing the patterns of retention of the imprinted compounds on the different MIPs when related to a blank (non-imprinted) polymer in a high performance liquid chromatography system. Furthermore, frontal analysis was carried out on three polymers: a blank, a pyridine-imprinted and a 4,4'-bipyridyl-imprinted polymer, to evaluate the number (Bt), average specificity and strength (dissociation constant; Kdiss) of the recognition sites. The Kdiss values of pyridine on the different polymers were in the range 0.10-0.12 M, and the amount of imprinted binding sites (Bt) 0.10-0.12 mmol/g. Kdiss values of 4,4'-bipyridyl were approximately 0.06 M, with Bt values equal to the above, except for in the anti-4,4'-bipyridyl polymer where the Kdiss was determined to be 0.02 M and Bt 0.07 mmol/g. From the results it can be concluded that multiple additive weak interactions dominate the recognition of the template molecules in these imprinted polymers.

Binding Sites↗

Chiral recognition in adrenergic receptor binding mimics prepared by molecular imprinting.

Molecularly imprinted polymers were prepared against the adrenomimetic agents ephedrine and pseudoephedrine. These compounds each incorporate two chiral centres. The polymers were evaluated with respect to enantiodiscrimination of various adrenergic ligands. The selectivity of the polymeric binding sites for the imprinted molecules was very high, and it was found that binding of both the enantiomeric and diastereomeric isomers of the imprint species were effectively obstructed, it was found that these polymers could selectively recognize the enantiomers of the endogenous adrenergic ligand epinephrine as well as several beta-adrenergic blockers. These observations suggest that these polymers effectively mimic the recognition patterns exhibited by natural adrenergic receptors.

Adrenergic Agents↗

An approach towards surface imprinting using the enzyme ribonuclease A.

An adsorbent showing enhanced selectivity for the enzyme RNase A was prepared by a surface imprinting procedure based on metal coordination. A metal chelating monomer, N-(4-vinyl)-benzyl iminodiacetic acid, was polymerized onto methacrylate-derivatized silica particles in the presence of RNase A and metal ions. Lysozyme and RNase A were separated on the adsorbent used as stationary phase in high-performance liquid chromatography.

Adsorption↗