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Query: CAS:61191-21-7 (2-butanone)
 604 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The presence of a proteinase in the composition of the ribosomal proteins of rat liver is demonstrated. The enzyme possesses optimal activity in the zone of pH 7.0-7.2. Soybean trypsin inhibitor and 1-chloro-4-phenyl-3-tosylamido-2-butanone inhibit the enzyme by 50-60%.
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PMID:Presence of a proteinase in polyribosomes of rat liver. 1 8

Phenylacetone, phenyl-2-butanone, and 3-methyl-1-phenyl-2-butanone were incubated with rabbit liver 9000g supernatant fraction for 30 and 60 min to yield primarily the alcohols, plus small amounts of 1,2-glycols and ketols (2-one-1-ols). Phenylacetone incubations produced small amounts of benzoic acid, which was confirmed as a true metabolite by incubation of 2H5 (phenyl-labeled) phenylacetone and corresponding recovery of phenyl-labeled benzoic acid. No benzoic acid was detectable from incubations of phenyl-2-butanone and 3-methyl-1-phenyl-2-butanone. 3-Methyl-1-phenyl-2-butanone yielded eight metabolites in addition to the corresponding alcohol, and structures are proposed for some of these metabolic products.
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PMID:In vitro metabolism of phenylacetone, phenyl-2-butanone, and 3-methyl-1-phenyl-2-butanone by rabbit liver preparations. 2 19

Cultures of methane- or methanol-utilizing microbes, including obligate (both types I and II) and facultative methylotrophic bacteria, obligate methanol utilizers, and methanol-grown yeasts were isolated from lake water of Warinanco Park, Linden, N.J., and lake and soil samples of Bayway Refinery, Linden, N.J. Resting-cell suspensions of these, and of other known C1-utilizing microbes, oxidized secondary alcohols to their corresponding methyl ketones. The product methyl ketones accumulated extracellularly. Succinate-grown cells of facultative methylotrophs did not oxidize secondary alcohols. Among the secondary alcohols, 2-butanol was oxidized at the highest rate. The optimal conditions for in vivo methyl ketone formation were compared among five different types of C1-utilizing microbes. Some enzymatic degradation of 2-butanone was observed. The product, 2-butanone, did not inhibit the oxidation of 2-butanol. The rate of the 2-butanone production was linear for the first 4 h of incubation for all five cultures tested. A yeast culture had the highest production rate. The optimum temperature for the production of 2-butanone was 35 degrees C for all the bacteria tested. The yeast culture had a higher temperature optimum (40 degrees C), and there was a reasonably high 2-butanone production rate even at 45 degrees C. Metal-chelating agents inhibit the production of 2-butanone, suggesting the involvement of metal(s) in the oxidation of secondary alcohols. Secondary alcohol dehydrogenase activity was found in the cell-free soluble extract of sonically disrupted cells. The cell-free system requires a cofactor, specifically nicotinamide adenine dinucleotide, for its activity. This is the first report of a nicotinamide adenine dinucleotide-dependent, secondary alcohol-specific enzyme.
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PMID:Microbial oxidation of gaseous hydrocarbons: production of methyl ketones from their corresponding secondary alcohols by methane- and methanol-grown microbes. 3 3

Cell suspensions of yeasts, Candida utilis ATCC 26387, Hansenula polymorpha ATCC 26012, Pichia sp. NRRL-Y-11328, Torulopsis sp. strain A1, and Kloeckera sp. strain A2, grown on various C-1 compounds (methanol, methylamine, methylformate), ethanol, and propylamine catalyzed the oxidation of secondary alcohols to the corresponding methyl ketones. Thus, isopropanol, 2-butanol, 2-pentanol, and 2-hexanol were converted to acetone, 2-butanone, 2-pentanone, and 2-hexanone, respectively. Cell-free extracts derived from methanol-grown yeasts catalyzed an oxidized nicotinamide adenine dinucleotide-dependent oxidation of secondary alcohols to the corresponding methyl ketones, Primary alcohols were not oxidized. The effect of various environmental factors on the production of methyl ketones from secondary alcohols by methanol-grown Pichia sp. was investigated.
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PMID:Oxidation of secondary alcohols to methyl ketones by yeasts. 4 48

In West Berlin in the autumn of 1975 through the following 5 months we observed 18 juvenile patients who had a toxic polyneuropathy and had sniffed a glue thinner. The neurological picture consisted of a symmetrical, progressive, ascending, mainly motor, polyneuropathy with pronounced muscle atrophy and characteristic vegetative alterations. The height of the disease was reached after 1 1/2-2 1/2 months and was characterized by tetraplegia in 7 patients. After 8 months all patients still had a motor deficit. Nerve biopsy showed paranodal axon swelling, dense masses of neurofilaments and secondary myelin retraction. The neurological and morphological data correspond to the "glue sniffer's neuropathy" and the n-hexane and MBK polyneuropathy after industrial exposure, as described in 10 cases to date. However, there was no MBK in the glue thinner. The polyneuropathies occurred in close time relation with the denaturation of the thinner with MEK (2-butanone). It is concluded from the data n-hexane and MBK have a common toxic mechanism with primary axonal changes and that there is an additional synergistic effect of MEK.
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PMID:Toxic polyneuropathies after sniffing a glue thinner. 6 97

Homozygous second chromosome lines were extracted from a natural population of Drosophila melanogaster and tested for their olfactory responses to ethyl acetate. The chromosome lines were highly heterogeneous for this behavior, and the variability was also specific to other esters and ketones such as ethyl propionate, 2-butanone, 2-pentanone, and 3-pentanone. The responses to these odorants negatively correlated with the response to another odorant, lactic acid. A large part of this odorant-specific variation seemed to be controlled by genes located on the right arm of the second chromosome.
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PMID:Behavior genetics of olfactory responses in Drosophila. II. An odorant-specific variant in a natural population of Drosophila melanogaster. 10 3

The synthesis of 11-thiohomofolic acid (2) has been accomplished by an unambiguous procedure. Reaction of 1-chloro-4-[p-(carbomethoxy)thiophenoxy]-2-butanone (10) with hydroxylamine under carefully controlled conditions gave the corresponding oxime 33. Conversion of this oxime to 1-phthalimido-4-[p-(carbomethoxy)thiophenoxy]-2-butanone oxime (4) was carried out by its reaction with potassium phthalimide using crown 18 ether as a catalyst. Hydrazinolysis of compound 4 gave 1-amino-4-[p-(carbomethoxy)thiophenoxy]-2-butanone oxime (5), which was used for the construction of the title compound 2 by modification of the Boon and Leigh procedure. An alternate synthesis utilizing 1-hydroxy-4-[p-(carbomethoxy)thiophenoxy]-2-butanone (11) and 4-hydroxy-2,5,6-triaminopyrimidine has also been carried out. Compound 2 did not exhibit any antifolate activity against Lactobacillus casei or Streptococcus faecium. The dithionite reduction product, 7,8-dihydro-11-thiohomofolic acid, was able to function as a substrate of L. casei dihydrofolate reductase. The catalytic reduction product of 2, consisting of a mixture of diastereomers, exhibited powerful antifolate activity against both these organisms.
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PMID:Folate analogues altered in the C9-N10 bridge region: 11-thiohomofolic acid. 10 15

YG 19-256, 4-(1,3,4,9b-tetrahydro-5 methyl-2H-indeno[1,2-c]pyridine-2-yl)-2-butanone methane sulphonate, 1-3 mg/kg i.v., abolished or reduced photically-induced myoclonic responses for 1.5-6.5 h in baboons, Papio papio, without producing signs of acute neurological toxicity.
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PMID:Anticonvulsant action of YG 19-256 in baboons with photosensitive epilepsy. 11 64

MEK (2-butanone) when combined with MBK (2-hexanone) markedly enhanced MBK neurotoxicity. MBK in rat plasma after exposure to MBK/MEK increased with time. Metabolites of MBK identified in blood and urine of rats and guinea pigs were 2-hexanol and 2,5-hexanedione.
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PMID:Toxicity and metabolism of methyl n-butyl ketone. 17 51

Cell-free extracts derived from yeasts Candida utilis ATCC 26387, Hansenula polymorpha ATCC 26012, Pichia sp. NRRL-Y-11328 Torulopsis sp. strain A1 and Kloeckera sp. strain A2 catalyzed an NAD+-dependent oxidation of secondary alcohols (2-propanol, 2-butanol, 2-pentanol, 2-hexanol) to the corresponding methyl ketones (acetone, 2-butanone, 2-pentanone, 2-hexanone). We have purified a NAD+-specific secondary alcohol dehydrogenase from methanol-grown yeast, Pichia sp. The purified enzyme is homogenous as judged by polyacrylamide gel electrophoresis. The purified enzyme catalyzed the oxidation of secondary alcohols to the corresponding methyl ketones in the presence of NAD+ as an electron acceptor. Primary alcohols were not oxidized by the purified enzyme. The optimum pH for oxidation of secondary alcohols by the purified enzyme is 8.0. The molecular weight of the purified enzyme as determined by gel filtration is 98 000 and subunit size as determined by sodium dodecyl sulfate gel electrophoresis is 48 000. The activity of the purified secondary alcohol dehydrogenase was inhibited by sulfhydryl inhibitors and metal-binding agents.
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PMID:Microbial production of methyl ketones. Purification and properties of a secondary alcohol dehydrogenase from yeast. 23 31


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