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PubMed1987

High and low molecular weight tracers for the electron microscopical detection of sialoglycoconjugates.

Hydrazide-derivative tracers of different molecular weights have been synthesized for use in the electron microscopical detection of sodium periodate-oxidized sialyl residues of glycoconjugates in various tissues and cells. Haemundecapeptide hydrazide, horseradish peroxidase hydrazide, and Limulus polyphemus haemocyanin hydrazide were obtained by coupling adipic acid dihydrazide to the tracers with the aid of water-soluble carbodiimide. The enzymatic tracers thus prepared retained their peroxidatic activity. On conversion to the hydrazide derivative, the haemocyanin molecule dissociated into its hexameric subunits. In order to test by transmission electron microscopy the ability of the conjugates to bind to the sialoglycoconjugates of endothelial cell surfaces, each tracer was perfused in situ into rat pancreatic vasculature previously oxidized with 1 mM sodium periodate. The three tracers characteristically labelled the various microdomains of the luminal cell coat of the capillary endothelial cell. The electron opacity of the haemocyanin subunits allowed their easy detection when bound to the cell surface or to components of the extracellular matrix. The bound markers were not displaced by a high ionic strength buffer, and did not label desialylated cell surfaces. These results indicate that the three hydrazide-derivative tracers may be useful tools for the electron microscopical detection of cellular and extracellular sialoglycoconjugates.

Animals↗
PubMed1980

Biochemical studies in the cerebro-hepato-renal syndrome of Zellweger: a disturbance in the metabolism of pipecolic acid.

The metabolism of pipecolic acid ahs been studied in three patients suffering from the cerebro-hepato-renal syndrome of Zellweger. A marked pipecolic aciduria was observed in these patients and serum levels of pipecolic acid were also elevated. From in vivo studies evidence was obtained that a disturbance in the catabolic pathway of pipecolic acid was present in all patients. This conclusion was based on the delayed return of the serum pipecolic acid concentration to the fasting concentration after oral loading of the patients with DL-pipecolic acid. Moreover, no increase in the excretion of alpha-amino adipic acid was observed in the patients after loading, in contrast with the control subjects, who showed a marked increase in the excretion of this metabolite of pipecolic acid. Further evidence for the presence of a metabolic defect in the catabolism of pipecolic acid was obtained from the observation that patients excreted significantly higher amounts of pipecolic acid during the loading experiment.

Amino Acids↗
PubMed1980

Alpha-aminoadipic aciduria: chemical and enzymatic studies.

A new case of alpha-aminoadipic aciduria had an apparent immunodeficiency and died at the age of 4 months. The urine contained large amounts of alpha-aminoadipate and smaller quantities of alpha-keto- and alpha-hydroxyadipate. Post mortem, the highest concentrations of alpha-aminoadipate were found in liver and kidney. Enzymatic studies on liver and cultured fibroblasts failed to demonstrate the expected deficiency of alpha-amino-adipate aminotransferase, a result perhaps explicable by the presence of cytoplasmic aminotransferase activity.

2-Aminoadipic Acid↗
PubMed1996

Methylmalonic and malonic aciduria in a dog with progressive encephalomyelopathy.

A 12 week old female Labrador retriever dog with signs of progressive diffuse degeneration of the brain and spinal cord was found to have methylmalonic and malonic aciduria. Over a 5 month period, the dog developed neurologic signs compatible with disease of the central nervous system with predominant diffuse cerebral and right lateralizing brainstem deficits. Gross pathological examination of the brain showed that the lateral, third, and fourth ventricles of the brain were markedly enlarged and associated with white and grey matter atrophy. Syringomyelia and hydromyelia of the central canal into the dorsal funiculus of the spinal cord beginning at the level of the cervical intumescence and extending to the lumbar intumescence was also present. Significant biochemical abnormalities include methylmalonic and malonic aciduria, mild lactic and pyruvic aciduria. There was also accumulation of citric acid cycle intermediates including succinic, aconitic, and fumaric acids. Disordered fatty acid oxidation was suggested by increased excretion of adipic, ethylmalonic, suberic and sebacic acids. Neither ketoacidosis nor hyperammonemia were present, and serum cobalamin levels were normal. Overall, this dog demonstrates an inborn error of metabolism resulting in abnormal organic acid accumulation associated with a neurodegenerative disease.

Animals↗
PubMed1980

Biochemical studies in a patient with defects in the metabolism of acyl-CoA and sarcosine: another possible case of glutaric aciduria type II.

The clinical and biochemical abnormalities in a neonate, who died in coma accompanied by severe hypoglycaemia at the age of 3 days, are described. The study of the urinary metabolic profiles of organic acids and amino acids revealed that the excretion rates of glutaric acid, isovaleric acid, isovalerylglycine, 3-hydroxyisovaleric acid and isobutyric acid were very high. Increased excretion rates were also found for 2-methylbutyric acid, adipic acid, caproylglycine, 5-hydroxycaproic acid, caproic acid and butyric acid. The amino acid, sarcosine, was excreted in enhanced amounts and the patient had lactic aciduria, whereas the excretion of 3-hydroxybutyric acid was only moderately increased. This abnormal excretion pattern is consistent with a defect in the metabolism of acyl-CoAs and sarcosine. Normal activity of glutaryl-CoA dehydrogenase was found, excluding glutaryl-CoA dehydrogenase deficiency (glutaric aciduria type I).

Acyl Coenzyme A↗
PubMed1995

Metabolism of cyclohexane carboxylic acid by the photosynthetic bacterium Rhodopseudomonas palustris.

Cyclohexane carboxylate supported relatively rapid growth (doubling times 7-8 h) of Rhodopseudomonas palustris under oxic or photosynthetic conditions, but did not serve as a substrate for either of the known aromatic CoA ligases. A CoA ligase that thioesterifies cyclohexane carboxylate was partially purified and did not cross react immunologically with the two CoA ligases purified previously from this bacterium. Crude extracts of R. palustris cells grown with a range of aromatic or alicyclic acids contained a dehydrogenase that reacted with cyclohexane carboxyl-CoA or cyclohex-1-ene carboxyl-CoA, using 2,6-dichlorophenolindophenol or ferricenium ion as electron carrier. This activity was not detected in extracts of adipate-, glutamate-, or succinate-grown cells. No oxidation or reduction of nonesterified cyclohexane carboxylate or cyclohexene carbocylate was detected in extracts of cells grown with aromatic or aliphatic substrates, neither aerobically nor anaerobically. A constitutively expressed thioesterase that hydrolyzed cyclohexane carboxyl-CoA and also some alicyclic and aliphatic CoA derivatives was purified and characterized. The enzyme had little or no activity on benzoyl-CoA or 4-hydroxybenzoyl-CoA. The presence of a thioesterase that effectively hydrolyzes cyclohexane carboxyl-CoA suggests that transient production of cyclohexane carboxylate is a physiological response to temporary excess of reductant during metabolism of aromatic compounds.

Amino Acid Sequence↗
PubMed1995

Comparative studies on the nephrotoxicity of 2-bromoethanamine hydrobromide in the Fischer 344 rat and the multimammate desert mouse (Mastomys natalensis).

Renal papillary necrosis (RPN) was induced in Fischer 344 (F344) rats (n = 4) using 2-bromoethanamine hydrobromide (BEA) dosed at 150 mg/kg, and in multimammate desert mice (Mastomys natalensis) at 150 and 250 mg/kg (n = 4 per group). Control rats and Mastomys were dosed with 0.9% saline (n = 4 per group). Urine was collected at regular intervals for up to 4 days post-dosing and analysed for low MW metabolites using high resolution 1H NMR spectroscopy. The urinary activity of lactate dehydrogenase, gamma-glutamyl transpeptidase and alkaline phosphatase was determined using conventional biochemical assays. On termination, histopathological examination of papillae was performed showing the development of extensive lesions in F344 rats at 150 mg/kg BEA. Mastomys appeared much more resistant to BEA and showed normal renal histology at 150 mg/kg and patchy lesions at 250 mg/kg BEA. Enzyme analysis of control urine showed F344 rats to have > 1000% higher gamma-glutamyl transpeptidase activity than Mastomys. 1H NMR spectroscopic analysis showed that BEA caused a substantial decrease in urinary concentrations of succinate and citrate (0-24 h p.d.) and an increase in creatine (0-96 h p.d.) in both animal models. A decrease in the urinary concentration of 2-oxoglutarate with a subsequent increase by 72-96 h p.d. was also noted in both animal models. Glutaric and adipic aciduria were also induced in both F344 rats and Mastomys 0-24 h post-BEA treatment, indicative of an enzyme deficiency in the acyl CoA dehydrogenases. Urinary taurine levels were elevated in Mastomys following the administration of BEA, indicating some degree of liver toxicity. Urinary taurine was not elevated in F344 rats following BEA administration, demonstrating further species difference in BEA toxicity.

Animals↗
PubMedDate not supplied

Glucoamylase immobilization on a magnetic microparticle for the continuous hydrolysis of maltodextrin in a fluidized bed reactor.

Glucoamylase (GA) has been successfully immobilized through its carbohydrates previously oxidized with periodate onto a low-cost magnetic microparticle made of polyethyleneimine-coated magnetite crosslinked with glutaraldehyde (M-GAD) and derivatized with adipic dihydrazide (ADH). A stabilization posttreatment consisting of crosslinking its carbohydrates with ADH, increased the remaining activity from 54 to 71%, calculated on the Vm values and measured at 50 degrees C and pH 4.5 with maltodextrin (DE 11-14) as substrate. This treatment also improved the enzyme stability and lowered the deactivation rate constant kd to a third of its value. A 30% maltodextrin solution has been continuously hydrolyzed at 50 degrees C and pH 4.5 in a recycled, fluidized bed reactor (FBR) containing GA immobilized on these magnetic microparticles. They easily settled in this highly viscous medium because of their high density (5 g/mL), and washout of ultrafines was prevented by surrounding the top of the bed with an electromagnet. The small particle size (20 microns) allowed a high enzyme loading in the reactor and also a high bed voidage, which is recommended to avoid extensive pressure drop and consequent channeling problems. The kinetic of hydrolysis fitted with the plug-flow model; this is explained by the insignificant backmixing effects observed. After 2 wk of hydrolysis under process conditions leading to a conversion of 70%, which corresponds to a high-conversion syrup, the immobilized GA only lost 4% of its initial activity.

Biosensing Techniques↗
PubMed1984

Gas chromatography--mass spectrometry (GC--MS) diagnosis of two cases of medium chain acyl-CoA dehydrogenase deficiency.

Two patients with hypoketotic hypoglycaemia and dicarboxylic aciduria are described. Studies of their urinary organic acids by gas chromatography-mass spectrometry (GC-MS) showed an excretion of dicarboxylic acids (adipic suberic and sebacic acids), unsaturated dicarboxylic acids (cis-octenedioic and decenedioic acids),5-hydroxyhexanoic acid, hexanoyl-glycine and suberylglycine. Deficiency of the medium chain acyl-CoA dehydrogenase (MCAD) in fibroblasts was documented for both children. Despite a similar presentation (hypoglycaemic coma), organic acid profile (dicarboxylic aciduria and suberylglycine excretion) and enzyme deficiency (MCAD), they did not respond similarly to glucose infusion.

Acyl-CoA Dehydrogenase↗
PubMed1998

A unique fungal lysine biosynthesis enzyme shares a common ancestor with tricarboxylic acid cycle and leucine biosynthetic enzymes found in diverse organisms.

Fungi have evolved a unique alpha-amino-adipate pathway for lysine biosynthesis. The fungal-specific enzyme homoaconitate hydratase from this pathway is moderately similar to the aconitase-family proteins from a diverse array of taxonomic groups, which have varying modes of obtaining lysine. We have used the similarity of homoaconitate hydratase to isopropylmalate isomerase (serving in leucine biosynthesis), aconitase (from the tricarboxylic acid cycle), and iron-responsive element binding proteins (cytosolic aconitase) from fungi and other eukaryotes, eubacteria, and archaea to evaluate possible evolutionary scenarios for the origin of this pathway. Refined sequence alignments show that aconitase active site residues are highly conserved in each of the enzymes, and intervening sequence sites are quite dissimilar. This pattern suggests strong purifying selection has acted to preserve the aconitase active site residues for a common catalytic mechanism; numerous other substitutions occur due to adaptive evolution or simply lack of functional constraint. We hypothesize that the similarities are the remnants of an ancestral gene duplication, which may not have occurred within the fungal lineage. Maximum likelihood, neighbor joining, and maximum parsimony phylogenetic comparisons show that the alpha-aminoadipate pathway enzyme is an outgroup to all aconitase family proteins for which sequence is currently available.

Aconitate Hydratase↗
PubMed2003

Dietary elevated sucrose modulation of diesel-induced genotoxicity in the colon and liver of Big Blue rats.

Earlier studies have indicated that sucrose possesses either co-carcinogenic or tumor-promoter effects in colon carcinogenesis induced by genotoxic carcinogens. In this study we investigated the role of sucrose on diesel exhaust particle (DEP)-induced genotoxicity in the colonic mucosa and liver. Big Blue rats were fed with DEP (0.8 ppm in feed) and/or sucrose (3.45% or 6.85% w/w in feed) for 3 weeks. DEP increased both DNA strand breaks and DNA adducts in colon. Interestingly, sucrose also increased the level of bulky DNA adducts in colon. DEP and sucrose had no effect on DNA strand-breaks and DNA adducts in liver. DEP and sucrose treatment did not have any effect on mutation frequency in colon and liver. Oxidative DNA damage detected as 8-oxodG (8-oxo-7,8-dihydro-2'-deoxyguanosine) and endonuclease III or formamidopyrimidine DNA glycosylase sensitive sites was unaltered in colon and liver. The mRNA expression levels of the DNA repair enzymes N-methylpurine DNA glycosylase ( MPG), 8-oxoguanine DNA glycosylase ( OGG1) and ERCC1 (part of the nucleotide excision repair complex) measured by reverse transcription-polymerase chain reaction were increased in liver by DEP feeding. In colon, expression was unaffected by DEP or sucrose feeding. Among biomarkers of oxidative stress, including vitamin C, malondialdehyde and protein oxidations (gamma-glutamyl semialdehyde and 2-amino adipic semialdehyde) in plasma and liver, only malondialdehyde was increased in plasma by sucrose/DEP feeding. In conclusion, sucrose feeding did not increase DEP-induced DNA damage in colon or liver.

Animals↗
PubMed1999

Technetium-99m somatostatin analogues: effect of labelling methods and peptide sequence.

In this paper the preclinical evaluation of the somatostatin analogue RC160 labelled with technetium-99m using bifunctional chelators (BFCs) based on the hydrazinonicotinamide (HYNIC) and N(3)S system is described and a comparison made with [Tyr(3)]-octreotide (TOC). Conjugates of both peptides with HYNIC, and of RC160 with benzoyl-MAG(3) and an N(3)S-adipate derivative were prepared and radiolabelling performed at high specific activities using tricine, tricine/nicotinic acid and ethylenediamine-N,N'-diacetic acid (EDDA) as co-ligands for HYNIC conjugates. All conjugates and (99m)Tc-labelled peptides showed preserved binding affinity for the somatostatin receptor (IC50, Kd<5 nM). The biodistribution was markedly dependent on the BFC and co-ligand used, with the amidothiol ligands showing a greater degree of hepatobiliary clearance, the HYNIC/tricine complex higher blood levels and the HYNIC/EDDA complex the highest level of renal excretion and lowest blood levels. All peptide conjugates showed receptor-mediated uptake in tumour xenografts, but tumour uptake was significantly lower for the (99m)Tc-RC160 derivatives compared with (99m)Tc-EDDA/HYNIC-[Tyr(3)]-octreotide (0.2%-3.5%ID/g vs 9.7%ID/g) and correlated well with the reduced internalisation rate for RC160 derivatives. Our results show that the selection of the labelling approach as well as the right choice of the peptide structure are crucial for labelling peptides with (99m)Tc to achieve complexes with favourable biodistribution. Despite the relatively low tumour uptake compared with (99m)Tc-EDDA/HYNIC-[Tyr(3)]-octreotide, (99m)Tc-RC160 could play a role in imaging tumours that do not bind octreotide derivatives.

Animals↗
PubMed2006

Synthesis of alpha-trifluoromethyl alpha-amino acids with aromatic, heteroaromatic and ferrocenyl subunits in the side chain.

5-Benzyloxy-4-trifluoromethyl-1,3-oxazoles, obtained from 5-fluoro-4-trifluoromethyloxazoles and benzyl alcohols, are capable for rearrangements. A 1,3 shift of a benzyl group is the key step of a new general route toward alpha-trifluoromethyl substituted aromatic and heteroaromatic amino acids, demonstrating that 5-fluoro-4-trifluoromethyl-1,3-oxazole is a synthetic Tfm-Gly equivalent. On reaction with benzpinacol partially fluorinated oxazoles are transformed into bis(trifluoromethyl) substituted 2,5-diamino adipic acid and N-benzoyl-2-benzhydryl-3,3,3-trifluoroalanine.

Amino Acids↗
PubMed2007

Molecular model for host–guest interaction of tetraamino-tert-butylthiacalix[4]arene and tetraamino-tert-butylcalix[4]arene receptors with carboxylate and dicarboxylate guests: an ONIOM study.

Geometry optimizations of tetraamino-tert-butylthiacalix[4]arene (tatbtc4a) and tetraamino-tert-butylcalix[4]arene (tatbc4a) complexes with acetate, oxalate,malonate, succinate, glutarate, adipate, and pimelate were carried out using the integrated MO:MO method. Thermodynamic quantities, preorganization energies and complexation energies of these complexes were obtained at the ONIOM(B3LYP/6-31G(d):AM1) level of theory. The relative stabilities of the tatbtc4a and tatbc4a complexes with carboxylate guests are reported. The complexes tatbtc4a/malonate and tatbc4a/oxalate were found to be the most stable species. The selectivity of the tatbtc4a receptor toward to malonate with respect to oxalate, in terms of selectivity coefficient, K(oxalatemalonate) is 9.90×10(2).

Calixarenes↗
PubMed2006

A novel PHB depolymerase from a thermophilic Streptomyces sp.

A novel PHB depolymerase from a thermophilic Streptomyces sp. MG was purified to homogeneity by hydrophobic interaction chromatography and gel filtration. The molecular mass of the purified enzyme was 43 kDa as determined by size exclusion chromatography and 41 kDa by SDS-PAGE. The optimum pH and temperature were 8.5 and 60 degrees C respectively. The enzyme was stable at 50 degrees C and from pH 6.5-8.5. The enzyme hydrolyzed not only bacterial polyesters, i.e. poly(3-hydroxybutyric acid and poly(3-hydroxybutyrate-co-3-hydroxyvalerate), but also synthetic, aliphatic polyesters such as polypropiolactone, poly(ethylene adipate) and poly(ethylene succinate).

Acyltransferases↗
PubMed1987

Tresyl activation of a hydroxyalkyl ligand for coupling to a hydrazide gel: stable immobilization of T-2 toxin for affinity purification of T-2 antibody.

A stable T-2 hydrazide gel is prepared by activating T-2 toxin with tresyl chloride followed by coupling to agarose-adipic acid hydrazide. Utilized as an affinity chromatography column, this T-2 hydrazide gel purifies a monoclonal antibody for T-2 in high yield directly from ascites fluid. Specific antibody trapped on the column is eluted either with excess T-2 or at pH 11.6. Much less successful are two other T-2 affinity columns that were prepared and evaluated: T-2 bovine serum albumin Affi-Gel 15 and T-2 hexylamine Sepharose.

Antibodies↗
PubMed1987

Use of fluorescein hydrazide and fluorescein thiosemicarbazide reagents for the fluorometric determination of protein carbonyl groups and for the detection of oxidized protein on polyacrylamide gels.

Highly fluorescent thiosemicarbazide and hydrazide prepared by reaction of fluorescein isothiocyanate with hydrazine or adipic acid dihydrazide have been used to monitor the presence of carbonyl groups in oxidatively modified proteins. After oxidation, proteins react with these reagents under anaerobic conditions in the dark to yield fluorescent protein conjugates (presumably thiosemicarbazones or hydrazones) which can be visualized as fluorescent bands following electrophoresis (0-4 degrees C) on lithium dodecyl sulfate-polyacrylamide gels. These reagents do not react with unoxidized proteins. The conjugates formed dissociate readily at room temperature but are fairly stable at pH 6-9, 0 degrees C. Current data suggest that these reagents will be useful in the detection and quantitation of oxidatively modified proteins in biological systems.

Electrophoresis, Polyacrylamide Gel↗
PubMed1992

Direct dye binding--a quantitative assay for solid-phase immobilized protein.

A direct dye-binding procedure was established for the quantification of protein after its immobilization on a solid phase, using IgG and BSA as model proteins. The assay, which in the range 0-5 mg protein/ml gel correlates well with indirect protein determination by A280 as well as determination of protein hydrolyzed from the gel, is based on a modified Bradford dye-binding assay. As the protein coupled to the gel binds the dye, a decrease in A465 of the supernatant is measured. Three solid supports commonly used for protein immobilization (Sepharose, Sephadex, Sephacryl) were found to be compatible with the dye-binding assay while nonspecific dye binding was found to HEMA gels. Protein was coupled to Sephacryl S-1000 using three different activation methods (aldehyde, hydrazine, and adipic acid dihydrazide). Artifactual dye-binding was not observed using any of the three different "linkers." The assay is easily carried out and represents a useful tool, e.g., when optimizing procedures for protein immobilization.

Coloring Agents↗