Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LEVULINIC ACID”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,279 records · Page 71Linked to original sources
PubMed1969

The occurrence of substances in human plasma capable of inducing the enzyme delta-aminolevulinate synthetase in liver cells.

We have demonstrated the presence, in the plasma of several patients with acute intermittent porphyria, of a substance which strongly induced the synthesis of porphyrins in chick embryo liver cells growing in primary culture. The induction response evoked by this humoral agent was in all respects similar to that elicited by drugs and hormones which are known to enhance porphyrin production by inducing the de novo formation of delta-aminolevulinate synthetase, the rate-limiting enzyme in this pathway. Inducing properties were not found in the plasma of normal individuals or in that from porphyric patients in remission. Significant inducing activity was, however, found in the plasma of some normal subjects ingesting drugs or contraceptive steroid mixtures. The occurrence of a potent inducer of delta-aminolevulinate synthetase in the plasma of certain porphyric patients may have clinical significance for these genetically susceptible individuals. It will also permit chemical characterization of those humoral agents which may be related to the episodic exacerbations of this hereditary liver disease.

Animals↗
PubMed1972

On the mechanism of action of vitamin B 12 . Model studies. Thermal rearrangement of methyl 3,3-dimethylglycidate to methyl levulinate.

The discovery that methyl 3,3-dimethylglycidate rearranges to methyl levulinate on heating is discussed in terms of its possible consequences for the mechanism of action of the coenzyme B(12)-dependent enzymes: methylmalonyl-CoA mutase (EC 5.4.99.2), glutamate mutase (EC 5.4.99.1), and a-methyleneglutarate mutase. It is also suggested that the proposed mechanism may provide a unifying link between the mechanism of action of the above enzymes and that of the coenzyme B(12)-dependent dioldehydrase and related enzymes.

Butyrates↗
PubMed2003

6-(Levulinyloxymethyl)-3-methoxy-2-nitrobenzoyl and 2-(levulinyloxymethyl)-5-methoxy-4-nitrobenzoyl groups as novel base-labile groups for 5'-hydroxy protection in solid-phase oligonucleotide synthesis.

The 6-(levulinyloxymethyl)-3-methoxy-2-nitrobenzoyl (LMMoNBz) and 2-(levulinyloxymethyl)-5-methoxy-4-nitrobenzoyl (LMMpNBz) groups were developed as novel base-labile groups for 5'-hydroxy protection in solid-phase oligonucleotide synthesis. A comparative study of the utility of LMMoNBz, LMMpNBz, and 2-(levulinyloxymethyl)-5-nitrobenzoyl (LMNBz) groups is described.

Chromatography, High Pressure Liquid↗