Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Cyclohexanones”

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 451 records · Page 25Linked to original sources
PubMed1977

Affinity labelling of alcohol dehydrogenases. Chemical modification of the horse liver and the yeast enzymes with alpha-bromo-beta(5-imidazolyl)-propionic acid and 1,3-dibromoacetone.

1. DL-alpha-Bromo-beta(5-imidazolyl)-propionic acid is a potential affinity labelling reagent for metallo-enzymes. It has been used with the alcohol dehydrogenases from liver and yeast. The liver enzyme is chemically modified and inactivated in a Michaelis-Menten-type reaction, where one molecule of the reagent is bound per subunit. The enzyme is protected from the inhibitor in a competitive manner by imidazole, 2,2'-dipyridyl, 1,10-phenanthroline and cyclohexanone, which all combine with the active-site zinc. The protection by chloride, acetate and NADH, which are considered to bind at the general anion binding site, is not strictly competitive. Inactivation has an optimum at pH 8.5. For the liver enzyme, the reagent was found to decrease the initial rate of ethanol oxidation. Prior to the irreversible alkylation of Cys-46, reversible binding is shown to occur at the active-site zinc atom. The yeast enzyme was extremely resistant to the reagent and no specific modification was found. 2. The potential affinity labelling and crosslinking reagent, symmetrical 1,3-dibromoacetone although unstable, has also been used for chemical modification. With the liver enzyme, concentrations below 5 mM gave a reaction of the Michaelis-Menten-type at pH 7.0. Several ligands known to complex with the active-site region protect the enzyme against the reagent. Dibromoacetone gave rapid inactivation of the yeast enzyme. Despite the fact that a pseudo-first-order reaction was observed with respect to enzyme as well as inhibitor, no saturating effect was found. In this work, dibromoacetone reacted like a monofunctional reagent.

Acetone↗
PubMed1997

Stability assessment of lyophilized intravenous immunoglobulin after reconstitution in glass containers and poly(vinyl chloride) bags.

Human intravenous immunoglobulin (IGIV) has been in use for the past 20 years. This biological product is commonly provided in liquid or lyophilized dosage form. When the lyophilized product is rehydrated, it is usually administered within 2-3 h from time of complete dissolution. While this practice is advisable whenever possible, occasionally the patient or care-giver may need to delay the infusion. Hence, a study of the stability of lyophilized IGIV after reconstitution with water for injection was conducted. The reconstituted product was stored either in its original glass container or pooled into poly(vinyl chloride) (PVC) bags. The effect of extended storage on the active ingredient (IgG), excipients (glucose, albumin) and extractables [sodium from glass vials, and di-(2-ethyl-hexyl) phthalate and cyclohexanone from PVC bags] was evaluated. The stability of the active ingredient was evaluated by physico-chemical tests (molecularsize distribution, pH, appearance, total protein), monitoring titres of a specific antibody (hepatitis B surface antigen) and an antibody functional test (bacterial opsonization). To evaluate the risk of microbial contamination during reconstitution and pooling procedures, sterility, pyrogen and animal-safety tests were included in the protocol. The potential of IgG polymerizing in solution during storage and subsequent complement activation was evaluated by assaying for non-specific binding of complement (anti-complement activity). Results show that aseptically reconstituted IGIV is stable and remains sterile up to 48 h at 5 degrees C. The reconstituted product was also found to be stable at room temperature (25 degrees C) up to 12 h.

Drug Stability↗
PubMed1993

Structural requirements for the direct and cytochrome P450-dependent reaction of cyclic alpha,beta-unsaturated carbonyl compounds with glutathione: a study with coumarin and related compounds.

The interaction of glutathione (GSH) with coumarin, or one of a series of compounds related to coumarin, was assessed in the absence and presence of liver microsomes (direct reaction and indirect reaction, respectively) to determine the structural requirements for direct and mono-oxygenase-mediated reaction of cyclic alpha,beta-unsaturated carbonyls with GSH. Acrolein was used as a positive control for the direct reaction, and produced complete or nearly complete depletion of GSH under all assay conditions. 5,6-Dihydro-2H-pyran-2-one and 2-cyclohexen-1-one also produced substantial depletion of GSH in the direct reaction, which was not increased by the addition of liver microsomes. Coumarin, 2H-pyran-2-one and precocene I (a substituted pyran lacking the 2-one structure) were not substrates for the direct reaction but did cause depletion of GSH when incubated in the presence of rat or human liver microsomes. These depletions were dependent on a functioning mono-oxygenase system as judged by the effects of omission of cofactors, addition of competitive or inactivating inhibitors of cytochrome P450, and induction. Dihydrocoumarin, delta-valerolactone, cyclohexanone and 4H-pyran-4-one were not substrates for either the direct or indirect reaction. These findings are rationalized on the basis of a direct nucleophilic attack of GSH on the alpha,beta-centre of the alpha,beta-unsaturated carbonyl compounds, which is hindered by benzenoid resonance in coumarin and 2H-pyran-2-one, for which enzyme-mediated reaction with GSH, probably via a 3,4-epoxide, is the favoured mechanism.

Aged↗
PubMed1969

Giant hepatic mitochondria: production in mice fed with cuprizone.

Giant mitochondria in hepatocytes that have the average size of nuclei can be consistently produced in the liver of weanling mice by feeding them cuprizone (bis-cyclohexanone oxaldihydrazone). The simplicity of the procedure and the consistency of the results make the feeding of cuprizone a new and useful experimental tool for the study of mitochondrial metabolism.

Animals↗
PubMed1989

Survey of microbial oxygenases: trichloroethylene degradation by propane-oxidizing bacteria.

Microorganisms that biosynthesize broad-specificity oxygenases to initiate metabolism of linear and branched-chain alkanes, nitroalkanes, cyclic ketones, alkenoic acids, and chromenes were surveyed for the ability to biodegrade trichloroethylene (TCE). The results indicated that TCE oxidation is not a common property of broad-specificity microbial oxygenases. Bacteria that contained nitropropane dioxygenase, cyclohexanone monooxygenase, cytochrome P-450 monooxygenases, 4-methoxybenzoate monooxygenase, and hexane monooxygenase did not degrade TCE. However, one new unique class of microorganisms removed TCE from incubation mixtures. Five Mycobacterium strains that were grown on propane as the sole source of carbon and energy degraded TCE. Mycobacterium vaccae JOB5 degraded TCE more rapidly and to a greater extent than the four other propane-oxidizing bacteria. At a starting concentration of 20 microM, it removed up to 99% of the TCE in 24 h. M. vaccae JOB5 also biodegraded 1,1-dichloroethylene, trans-1,2-dichloroethylene, cis-1,2-dichloroethylene, and vinyl chloride.

Bacteria↗
PubMed1999

Screening, nucleotide sequence, and biochemical characterization of an esterase from Pseudomonas fluorescens with high activity towards lactones.

A genomic library of Pseudomonas fluorescens DSM 50106 in a lambdaRESIII phage vector was screened in Escherichia coli K-12 for esterase activity by using alpha-naphthyl acetate and Fast Blue RR. A 3.2-kb DNA fragment was subcloned from an esterase-positive clone and completely sequenced. Esterase EstF1 was encoded by a 999-bp open reading frame (ORF) and exhibited significant amino acid sequence identity with members of the serine hydrolase family. The deduced amino acid sequences of two other C-terminal truncated ORFs exhibited homology to a cyclohexanone monooxygenase and an alkane hydroxylase. However, esterase activity was not induced by growing of P. fluorescens DSM 50106 in the presence of several cyclic ketones. The esterase gene was fused to a His tag and expressed in E. coli. The gene product was purified by zinc ion affinity chromatography and characterized. Detergents had to be added for purification, indicating that the enzyme was membrane bound or membrane associated. The optimum pH of the purified enzyme was 7.5, and the optimum temperature was 43 degreesC. The showed highest purified enzyme activities towards lactones. The activity increased from gamma-butyrolactone (18.1 U/mg) to epsilon-caprolactone (21.8 U/mg) to delta-valerolactone (36.5 U/mg). The activities towards the aliphatic esters were significantly lower; the only exception was the activity toward ethyl caprylate, which was the preferred substrate.

Amino Acid Sequence↗
PubMed1999

Biodegradation of cyclohexylamine by Brevibacterium oxydans IH-35A.

A bacterial strain capable of growing on cyclohexylamine (CHAM) was isolated by using enrichment and isolation techniques. The strain isolated, strain IH-35A, was classified as a member of the genus Brevibacterium. The results of growth and enzyme studies are consistent with degradation of CHAM via cyclohexanone (CHnone), 6-hexanolactone, 6-hydroxyhexanoate, and adipate. Cell extracts obtained from this strain grown on CHAM contained CHAM oxidase, and the model for CHAM oxidation by this enzyme was similar to the model for deamino oxidation of amine by amine oxidase.

Biodegradation, Environmental↗
PubMed2002

Cloning and characterization of a gene cluster involved in cyclopentanol metabolism in Comamonas sp. strain NCIMB 9872 and biotransformations effected by Escherichia coli-expressed cyclopentanone 1,2-monooxygenase.

Cyclopentanone 1,2-monooxygenase, a flavoprotein produced by Pseudomonas sp. strain NCIMB 9872 upon induction by cyclopentanol or cyclopentanone (M. Griffin and P. W. Trudgill, Biochem. J. 129:595-603, 1972), has been utilized as a biocatalyst in Baeyer-Villiger oxidations. To further explore this biocatalytic potential and to discover new genes, we have cloned and sequenced a 16-kb chromosomal locus of strain 9872 that is herein reclassified as belonging to the genus COMAMONAS: Sequence analysis revealed a cluster of genes and six potential open reading frames designated and grouped in at least four possible transcriptional units as (orf11-orf10-orf9)-(cpnE-cpnD-orf6-cpnC)-(cpnR-cpnB-cpnA)-(orf3-orf4 [partial 3' end]). The cpnABCDE genes encode enzymes for the five-step conversion of cyclopentanol to glutaric acid catalyzed by cyclopentanol dehydrogenase, cyclopentanone 1,2-monooxygenase, a ring-opening 5-valerolactone hydrolase, 5-hydroxyvalerate dehydrogenase, and 5-oxovalerate dehydrogenase, respectively. Inactivation of cpnB by using a lacZ-Km(r) cassette resulted in a strain that was not capable of growth on cyclopentanol or cyclopentanone as a sole carbon and energy source. The presence of sigma(54)-dependent regulatory elements in front of the divergently transcribed cpnB and cpnC genes supports the notion that cpnR is a regulatory gene of the NtrC type. Knowledge of the nucleotide sequence of the cpn genes was used to construct isopropyl-beta-thio-D-galactoside-inducible clones of Escherichia coli cells that overproduce the five enzymes of the cpn pathway. The substrate specificities of CpnA and CpnB were studied in particular to evaluate the potential of these enzymes and establish the latter recombinant strain as a bioreagent for Baeyer-Villiger oxidations. Although frequently nonenantioselective, cyclopentanone 1,2-monooxygenase was found to exhibit a broader substrate range than the related cyclohexanone 1,2-monooxygenase from Acinetobacter sp. strain NCIMB 9871. However, in a few cases opposite enantioselectivity was observed between the two biocatalysts.

Catalysis↗
PubMed2000

Genetic analysis of a gene cluster for cyclohexanol oxidation in Acinetobacter sp. Strain SE19 by in vitro transposition.

Biological oxidation of cyclic alcohols normally results in formation of the corresponding dicarboxylic acids, which are further metabolized and enter the central carbon metabolism in the cell. We isolated an Acinetobacter sp. from an industrial wastewater bioreactor that utilized cyclohexanol as a sole carbon source. A cosmid library was constructed from Acinetobacter sp. strain SE19, and oxidation of cyclohexanol to adipic acid was demonstrated in recombinant Escherichia coli carrying a SE19 DNA segment. A region that was essential for cyclohexanol oxidation was localized to a 14-kb fragment on the cosmid DNA. Several putative open reading frames (ORFs) that were expected to encode enzymes catalyzing the conversion of cyclohexanol to adipic acid were identified. Whereas one ORF showed high homology to cyclohexanone monooxygenase from Acinetobacter sp. strain NCIB 9871, most of the ORFs showed only moderate homology to proteins in GenBank. In order to assign functions of the various ORFs, in vitro transposon mutagenesis was performed using the cosmid DNA as a target. A set of transposon mutants with a single insertion in each of the ORFs was screened for cyclohexanol oxidation in E. coli. Several of the transposon mutants accumulated a variety of cyclohexanol oxidation intermediates. The in vitro transposon mutagenesis technique was shown to be a powerful tool for rapidly assigning gene functions to all ORFs in the pathway.

Acinetobacter↗
PubMed2000

Conversion of 4-hydroxyacetophenone into 4-phenyl acetate by a flavin adenine dinucleotide-containing Baeyer-Villiger-type monooxygenase.

An arylketone monooxygenase was purified from Pseudomonas putida JD1 by ion exchange and affinity chromatography. It had the characteristics of a Baeyer-Villiger-type monooxygenase and converted its substrate, 4-hydroxyacetophenone, into 4-hydroxyphenyl acetate with the consumption of one molecule of oxygen and oxidation of one molecule of NADPH per molecule of substrate. The enzyme was a monomer with an M(r) of about 70,000 and contained one molecule of flavin adenine dinucleotide (FAD). The enzyme was specific for NADPH as the electron donor, and spectral studies showed rapid reduction of the FAD by NADPH but not by NADH. Other arylketones were substrates, including acetophenone and 4-hydroxypropiophenone, which were converted into phenyl acetate and 4-hydroxyphenyl propionate, respectively. The enzyme displayed Michaelis-Menten kinetics with apparent K(m) values of 47 microM for 4-hydroxyacetophenone, 384 microM for acetophenone, and 23 microM for 4-hydroxypropiophenone. The apparent K(m) value for NADPH with 4-hydroxyacetophenone as substrate was 17.5 microM. The N-terminal sequence did not show any similarity to other proteins, but an internal sequence was very similar to part of the proposed NADPH binding site in the Baeyer-Villiger monooxygenase cyclohexanone monooxygenase from an Acinetobacter sp.

Acetophenones↗
PubMed1999

Raised concentrations of aldehyde lipid peroxidation products in premature infants with chronic lung disease.

AIM: To indicate the extent of lipid peroxidation induced by oxidative stress, by measuring aldehyde end products in biological samples. METHODS: A highly specific gas chromatography and mass spectrometry (GC/MS) method was used to measure plasma concentrations of aliphatic aldehydes within the first week of life in 13 premature infants who subsequently developed chronic lung disease (CLD) and 11 infants without CLD (non-CLD). The oxime-tert-butyldimethylsilyl derivatives of aldehydes were analysed using 2,2,6,6-d4-cyclohexanone as the internal standard. RESULTS: All of the aldehydes measured were raised in those infants with CLD compared with non-CLD infants. Plasma concentrations of heptanal, 2-nonenal, and 4-hydroxynonenal (HNE) were significantly increased in CLD infants on the day of birth, while the differences in all aldehydes between the two groups were not significant at 4-6 days of age. Logistic regression analysis showed that the increase in these three aldehydes within the first 24 hours of life independently showed significant associations with the development of CLD. In particular, an HNE concentration of > or = 200 nM on day 0 was the best predictor for the early detection of CLD (odds ratio = 32.0), followed by a 2-nonenal concentration of > or = 150 nM (odds ratio = 16.0). CONCLUSIONS: These findings suggest that lipid peroxidation may have a role in the pathogenesis of neonatal CLD.

Aldehydes↗
PubMed1982

A cyclohexanecarboxylic acid utilizing yeast: isolation, identification, and nutritional characteristics.

A yeast capable of utilizing cyclohexanecarboxylic acid as sole carbon and energy source, strain KUY-6A, was isolated from soil by enrichment cultures. Taxonomical studies indicated that strain KUY-6A was Trichosporon cutaneum. Strain KUY-6A grew on a number of carboxylic acids. Among the cyclic compounds tested, cyclohexanecarboxylic acid was the best substrate. Cyclopentanecarboxylic acid, cycloheptanecarboxylic acid, cyclopentanone, cyclohexanone, and cyclopentanol also supported growth. In addition, the organism used the monocarboxylic acids, butyric, valeric, and caproic; the dicarboxylic acids succinic, glutaric, adipic, pimelic, and suberic; and the aromatic acids, benzoic and o-, m-, and p-hydroxybenzoic. The yeast did not require any vitamins for growth, although thiamine gave slight stimulation. The cell dry weight yield was 0.75 g from 1 g cyclohexanecarboxylic acid used.

Cyclohexanecarboxylic Acids↗
PubMed1996

Characterization of partial anaerobic metabolic pathway for 2,4,6-trinitrotoluene degradation by a sulfate-reducing bacterial consortium.

The anaerobic degradative pathway for metabolism of 2,4,6-trinitrotoluene (TNT) by a consortium of Desulfovibrio spp. isolated from a creek sediment was studied. This consortium has the metabolic capability to degrade TNT to fatty acids. The growth of the consortium and the metabolism of TNT were greatly enhanced in the presence of an additional carbon source like pyruvate. The optimal concentration of pyruvate for the maximum rate of TNT degradation was 15-20 mM. Various intermediates of TNT metabolism were identified. The first step in the pathway was reduction of TNT to 4-amino-2,6-dinitrotoluene and 2-amino-4,6-dinitrotoluene, which were further reduced to 2,4-diamino,6-nitrotoluene. The next intermediate to appear in the culture medium was nitrobenzoic acid, followed by cyclohexanone, 2-methyl pentanoic acid, butyric acid, and acetic acid. A study using radiolabeled TNT showed that no CO2 was produced from TNT during metabolism. The mass balance of the radiolabeled study showed that 49.6% of the TNT was converted to acetic acid, 28% was assimilated into biomass as trichloroacetic acid precipitable materials, and the rest was distributed as various TNT intermediates. Most Desulfovibrio spp. are incomplete oxidizers that are unable to carry out the terminal oxidation of organic substrates. The major end product of TNT metabolism was acetic acid. The bacteria grew on all the TNT intermediates tested as sole source of carbon, except on acetic acid, confirming that the Desulfovibrio spp. have the enzymes necessary for complete degradation of TNT to acetate.

Acetic Acid↗
PubMed1992

Signal transduction by the erythropoietin receptor: evidence for the activation of phospholipases A2 and C.

Erythropoietin (Ep) is the peptide growth factor whose actions on the erythroid progenitor cell induce terminal differentiation. However, the intracellular signaling system that is activated by Ep is poorly understood. Our previous studies have implicated the lipoxygenase metabolites of arachidonic acid in the actions of Ep. In this study, we report an early (30 s to 5 min) increase in levels of two lipoxygenase metabolites: leukotriene B4 (LTB4; 3- to 5-fold) and 12-hydroxyeicosatetraenoic acid (12-HETE; 2-fold). These responses were blocked by an antibody to Ep, by lipoxygenase inhibitors, or by 1,6-di[O-(carbamoyl)cyclohexanone oxime]hexane (RHC80267), an inhibitor of diacylglycerol (DAG) lipase. RHC 80267 also significantly inhibited Ep-mediated proliferation. Ep induced the release of [3H]arachidonic acid from cellular phospholipids at 5 min and also increased DAG accumulation at 1 min with a maximum increase of 68.2% over control seen at 30 min. No increase in levels of inositol trisphosphate or phosphatidic acid was observed in response to Ep. Taken together, these data suggest that the signal transduction pathway of the Ep receptor includes the activation of phospholipases A2 and C, resulting in the liberation of DAG and arachidonate and the subsequent formation of LTB4 and 12-HETE.

12-Hydroxy-5,8,10,14-eicosatetraenoic Acid↗
PubMed1980

Thermoregulation in Telazol (CI-744)-anesthetized rhesus monkey (Macaca mulatta).

Seven Telazol (CI-744)-[Telazol is an experimental drug (Parke, Davis) composed of two ingredients in equal amounts by weight: tiletamine HCl, designated chemically as 2-(ethylamino)-2-(2-thienyl)cyclohexanone-HCl, and zolazepam HCl, designated as 4-(o-fluorophenyl)-6,8-dihydro-1,3,8-trimethylpyrazolo-3,4-e 1,4 diazepin-7(IH)-one monohydrochloride] anesthetized rhesus monkeys (Macaca mulatta) were exposed to ambient temperatures (Ta) of 15, 23, 29, 35, and 38 degrees C to evaluate the effect of this dissociative anesthetic agent on thermoregulation. Thermal equilibrium in both anesthetized and control animals at Ta 15 degrees C was through peripheral vasoconstriction and metabolic heat production (M); shivering increased M in the anesthetized group to 1.7 times the resting M of 41.4 W x m-2. Both groups at Ta 38 degrees C regulated body temperature by vasodilation and increased skin evaporative heat loss (Esk) due to sweating. Anesthetized animals increased Esk from 6.4 W x m-2 at Ta 29 degrees C to 32.5 W x m-2 at Ta 38 degrees C. Panting was not observed in either group. Effective tissue thermal conductance was lowest at Ta 15 and 23 degrees C (6.9 and 7.6 W x m2 x degrees C-1, respectively), and increased with Ta's above 23 degrees C (45.0 W x m-2 at Ta 38 degrees C). These results indicate that Telazol-anesthetized monkeys maintain thermal balance at ambient temperatures from 15 to 38 degrees C, and that Telazol induces little or no impairment of thermoregulation in rhesus monkeys.

Anesthesia↗
PubMed1975

A safe and fast-acting surgical anesthetic for use in the guinea pig.

Ketamine [dl-2-(o-chlorophenyl)-2-(methylamino)cyclohexanone] hydrochloride was used in conjunction with Acepromazine [10-3-(dimethylamino)-propyl]phenothiazin-2-yl-methyl ketone] Maleate to produce surgical depth anesthesia in guinea pigs. In tests with 97 animals, an intramuscular injection of 44 mg/kg ketamine hydrochloride plus 2 mg Acepromazine Maleate was found to be effective in producing a surgical level of anesthesia within 2 min after administration. The anesthetic state lasted for an average of 1.5 h and could be safely extended by supplemental administrations of the drugs. This anesthetic combination was found to be fast acting, safe, and easily controlled.

Acepromazine↗
PubMed1994

Purification and characterization of 5 alpha-dihydrotestosterone 3 beta-hydroxysteroid dehydrogenase from mature pig testicular cytosol.

NADPH-dependent 5 alpha-dihydrotestosterone 3 beta-hydroxysteroid dehydrogenase (3 beta-HSD) was purified to apparent homogeneity from mature pig testicular cytosol. The purified enzyme catalyzed the conversion of 5 alpha-dihydrotestosterone (5 alpha-DHT) to 5 alpha-androstane-3 beta, 17 beta-diol. The molecular weight was estimated to be 31 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 28 kDa by gel filtration chromatography, indicating that the native 3 beta-HSD is a monomer. The isoelectric point of the purified enzyme was 5.8 as determined by chromatofocusing. The purified enzyme reduced not only 5 alpha-DHT but also 5 beta-DHT, 5 alpha(or 5 beta)-androstanedione, 5 alpha(or 5 beta)-dihydroprogesterone, prostaglandin E1, 13,14-dihydro-15-keto-prostaglandin F2 alpha, glyceladehyde, xylose and glucuronic acid. Moreover, the enzyme reduced other carbonyl compounds including aromatic aldehydes, aromatic ketones and quinones such as 4-nitrobenzaldehyde, 4-benzoylpyridine, phenylglyoxal, cyclohexanone and 9,10-phenanthrenequinone at high rates when compared with steroids, prostaglandins and sugars. The purified enzyme was inhibited by AgNO3, SH-reagent, disulfiram, hexesterol, stilbestrol, disulfiram and divalent cations such as Cu2+, Hg2+, Cd2+ and Co2+. Furthermore, the enzymatic properties of the purified enzyme, including catalytic activity, inhibitory effects by various agents and immunological properties, were compared with those of 3 alpha/beta-HSD enzymes from pig testicular cytosol.

3-Hydroxysteroid Dehydrogenases↗
PubMed1994

Structural components of beta-eudesmol essential for its potentiating effect on succinylcholine-induced neuromuscular blockade in mice.

beta-Eudesmol, a sesquiterpenoid alcohol isolated from Atractylodes lancea rhizoma, potentiates the neuromuscular blocking effect of succinylcholine (SuCh). The potentiating effect is greater in diabetic muscles than in normal ones. To identify the structural components of beta-eudesmol contributing to this action, we examined the potentiating effect of newly synthesized tertiary alcohols related to beta-eudesmol in phrenic nerve-diaphragm muscle preparations of normal and alloxan-diabetic mice. Potentiating effects were exhibited by cyclohexylidene derivatives but not by cyclohexanone or cyclohexanol derivatives. The compound 2-(3-hydroxy-3-methylbutyl)cyclohexylidene exhibited a potentiating effect, but 3-(3-hydroxy-3-methylbutyl)cyclohexylidene did not. These results indicate that both the presence of an exo-methylene attached to a cyclohexane ring and the distance between the exo-methylene and the hydroxy group in beta-eudesmol are involved in the potentiating effect on SuCh-induced neuromuscular blockade.

Animals↗