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Results for “Aminoethylphosphonic Acid”

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At least 19 recordsLinked to original sources
PubMed1984

Microbial protein synthesis in cattle given roughage-concentrate and all-concentrate diets: the use of 2,6-diaminopimelic acid, 2-aminoethylphosphonic acid and 35S as markers.

Three steers, each fitted with a rumen cannula and a re-entrant cannula in the proximal duodenum, were offered diets consisting of a barley-based concentrate and chopped hay at a daily intake of 61 g/kg live weight0.75 given in three equal meals. The ratio, concentrate: hay was changed from 50:50 to 90:10 and then to 100:0 in successive periods of 12-18 weeks and the flow and composition of digesta at the duodenum was measured over 48-h periods on each dietary treatment. Samples of bacteria and protozoa were separated from rumen contents and the proportions of bacterial and protozoal nitrogen (N) in duodenal digesta were estimated using 2,6-diaminopimelic acid (DAPA) and 2-aminoethylphosphonic acid (AEP) as markers. On separate occasions, radioactive sulphur (35S) was infused into the rumen for 48 h and digesta collected over the final 24 h; the specific radioactivity of S in microbial and digesta fractions was used to estimate the proportions of microbial N. 35S gave reproducible and apparently reliable estimates of microbial protein formation: the proportion of microbial N in digesta was significantly higher (P less than 0.05) for the 50:50 diet than for the other treatments but the energetic efficiency of microbial protein formation did not differ significantly between diets. Estimates of bacterial N based on DAPA concentrations were highly variable and frequently impossibly high. It is suggested that many of the anomalous values were the result of non-representative sampling of the rumen microbial population and that this is particularly likely to occur when conditions within the rumen are unstable. AEP was found to be unsuitable as a marker for rumen protozoa as considerable concentrations of this substance were found also in rumen bacteria.

Aminoethylphosphonic Acid↗
PubMed1998

Phosphate starvation-independent 2-aminoethylphosphonic acid biodegradation in a newly isolated strain of Pseudomonas putida, NG2.

A strain of Pseudomonas putida that utilized the biogenic organophosphonate 2-aminoethylphosphonic acid as sole carbon and energy, nitrogen and phosphorus source contained 2-aminoethylphosphonic acid: pyruvate aminotransferase and phosphonoacetaldehyde hydrolase (phosphonatase) activities which were inducible by the presence of 2-aminoethylphosphonic acid in the culture medium, regardless of the phosphate status of the cells. Neither of these activities were induced in their phosphate-free or phosphate-replete medium in the absence of 2-aminoethylphosphonic acid. Alkaline phosphatase activity was induced in phosphate limited medium, however, indicating a phosphate-starvation inducible response. In Enterobacter aerogenes IFO 12010, 2-aminoethylphosphonate: pyruvate aminotransferase and phosphonatase activities were induced only when cells were both phosphate limited and supplied with 2-aminoethylphosphonic acid as sole phosphorus source for growth. Neither enzyme activity was induced in phosphate-replete medium, or in medium where both 2-aminoethylphosphonic acid and inorganic phosphate were supplied as sources of phosphorus. The results point to the presence of a substrate inducible 2-aminoethylphosphonic acid biodegradation pathway in the isolated strain of Pseudomonas putida. Uniquely, therefore, the pathway is not under pho regulon control in this strain.

Alkaline Phosphatase↗
PubMed1977

Phosphonoglycoprotein from Metridium senile--heterogeneity of glycoproteins containing aminoethylphosphonic acid.

1. After separation by SDS gel-chromatography, analysis of AEP-containing glycoproteins from M. senile, indicated 66% amino acids with 220 AEP res./1000 res. and 30% carbohydrate for high mol. wt (greater than 10(7) forms and 80% amino acids with 25-50 AEP res./1000 res. and 10% carbohydrate for low mol. wt (2-4 x 10(4) forms. 2. Uronic acids, sulfate, lipid, and sialic acids were absent. 3. Mild base digestion released AEP-hexosamine containing oligosaccharides and destroyed ser-thr residues in the high mol. wt components. 4. Phosphonoglycoproteins appear to be acidic connective tissue components with AEP linked to hexosamine containing oligosaccharide side chains.

Amino Acids↗
PubMed1989

Distribution of ciliatine (2-aminoethylphosphonic acid) and phosphonoalanine (2-amino-3-phosphonopropionic acid) in human tissues.

Ciliatine (2-aminoethylphosphonic acid) was detected in the human brain, heart, kidney, liver, intestine, spleen, adrenal glands, and aorta. Phosphonoalanine (2-amino-3-phosphonopropionic acid) was found in the human liver, intestine and spleen. Tissue homogenates were extracted with trichloroacetic acid and a chloroform-methanol mixture. After hydrolysis, each fraction was subfractionated by ion-exchange chromatography and examined by paper chromatography and electrophoresis using a specific ninhydrin-molybdate staining procedure to detect the phosphonic acids. The acids were found bound either to lipid or to protein; no free phosphonic acid was detected.

Adrenal Glands↗
PubMed1998

Reaction of alanine racemase with 1-aminoethylphosphonic acid forms a stable external aldimine.

(R)-1-Aminoethylphosphonic acid (L-Ala-P), a synthetic L-alanine analogue, has antibacterial activity and is a time-dependent inactivator of all purified Gram-positive bacterial alanine racemases that have been tested. L-Ala-P forms an external aldimine with the bound pyridoxal 5'-phosphate (PLP) cofactor, but is neither racemized nor efficiently hydrolyzed. To understand the structural basis of the inactivation of the enzyme by L-Ala-P, we determined the crystal structure of the complex between L-Ala-P and alanine racemase at 1.6 A resolution. The cofactor derivative in the inhibited structure tilts outward from the protein approximately 20 degrees relative to the internal aldimine. The phosphonate oxygens are within hydrogen bonding distance of four amino acid residues and two water molecules in the active site of the enzyme. L-Ala-P is an effective inhibitor of alanine racemase because, upon formation of the external aldimine, the phosphonate group interacts with putative catalytic residues, thereby rendering them unavailable for catalysis. Furthermore, this aldimine appears to be inappropriately aligned for efficient Calpha proton abstraction. The combination of these effects leads to a stable aldimine derivative and potent inactivation of alanine racemase by this compound.

Alanine Racemase↗
PubMed1989

Occurrence of 2-aminoethylphosphonic acid in feeds, ruminal bacteria and duodenal digesta from defaunated sheep.

A quantitative method of analysis for 2-aminoethylphosphonic acid (AEP) was developed using reverse-phase HPLC. The detection limit for AEP was 15 nM, and the detector response (peak area) was linear from AEP levels up to 100 microM (R = .99). Mean recovery of AEP added to strained ruminal fluid from faunated sheep was 98.2%. When AEP was added to a fermentation mixture at a concentration of 22.6 micrograms/ml, 78% disappeared during a 24-h incubation. 2-Aminoethylphosphonic acid was readily detected in preparations of mixed ruminal ciliate protozoa as well as in mixed and pure strains of ruminal bacteria, feedstuffs, and ruminal fluid and duodenal digesta from defaunated sheep. The occurrence of AEP in feed and bacterial hydrolysates was confirmed by organic phosphorus analyses. The concentration of AEP in mixed ruminal protozoa was three times greater than its concentration in mixed ruminal bacteria (4,304 vs 1,383 micrograms/g DM, respectively). The AEP values for pure ruminal bacterial cultures ranged from 733 micrograms/g DM in Bacteroides succinogenes B21a to 1,166 micrograms/g DM in Butyrivibrio fibrisolvens H17c. Ruminal fluid and duodenal digesta from defaunated sheep contained AEP concentrations of 30 micrograms/ml and 90 micrograms/g DM, respectively. The concentration of AEP in feedstuffs ranged from 25 micrograms/g DM in wheat straw to 263 micrograms/g DM in oats. Because AEP occurrence is not limited to ruminal ciliate protozoa, it is of little value as a marker for protozoal presence in or passage out of the rumen.

Aminoethylphosphonic Acid↗
PubMed1977

2-Aminoethylphosphonic acid metabolism in the rat.

Time course studies of the incorporation of radioactive 2-aminoethylphosphonic acid (AEP) into the tissues of rats demonstrated that maximum incorporation into the liver lipids occurred within 12 to 30 hr after injection, compared to 2 to 3 hr for the incorporation of phosphorylethanolamine. Little incorporation of AEP was observed in the other tissues investigated (heart, lung, spleen, adipose, kidney). The AEP was incorporated to the greatest extent into 1,2-diacylglyceryl-aminoethylphosphonate (diacylglyceryl-AEP), the phosphonate analogue of phosphatidylethanolamine, with some incorporation into the lyso derivative. Diacylglycerol-AEP apparently was not further metabolized by the rat; no methylation of diacylglyceryl-AEP to phosphonolecithin was observed. Subcellular fractionation was performed on the livers of rats who received (3)H-AEP 12,30,36, and 48 hr prior to sacrifice. The greatest amount of radioactivity was recovered in the soluble fractions. Lipid extraction was performed on the subcellular fractions, and most of the radioactivity present in the lipids was found in the microsomal fraction, with the next highest recovery in the mitochondrial and nuclear fractions

Aminoethylphosphonic Acid↗
PubMed1984

Synergistic antibacterial activity between L-norvalyl-L-1-aminoethylphosphonic acid and nocardicin A.

The phosphonopeptide L- norvalyl -L-1- aminoethylphosphonic acid [ Nva -Ala(P)] has been studied in combination with 12 beta-lactam antibiotics for activity against Pseudomonas aeruginosa. Nocardicin A was found to give the most potent synergistic combination with Nva -Ala(P). This interaction was widely observed in clinical isolates of P. aeruginosa in vitro and in a mouse septicemia model. Synergy was also observed in vitro and in vivo in several other species, including Proteus mirabilis, indole-positive Proteus spp., and Serratia marcescens. The interaction between Nva -Ala(P) and nocardicin A involved a strongly bacteriolytic mechanism. In addition, the individual components were complementary to one another in their action against organisms not showing synergy. These properties resulted in a broad spectrum of activity of the combination Nva -Ala(P) plus nocardicin A when used to treat experimental gram-negative bacterial infections.

Alanine↗
PubMed1990

[Kinetic characteristics and enantioselective action of penicillinase in the hydrolysis reaction of N-phenylacetyl derivatives of 1-aminoethylphosphonic acid and its esters].

Penicillin acylase from E. coli (EC 3.5.1.11) was found to hydrolyze N-phenylacetylated 1-aminoethylphosphonic acid and its esters. The enzyme preferentially converts the R-form of the substrates: the ratios of the bimolecular rate constants of penicillin acylasecatalyzed hydrolysis of R- and S-forms of 1-(N-phenylacetamino)-ethylphosphonic acid and its dimethyl- and diisopropyl-esters are 58000, 2300, 1800; these derivatives were shown to have the greatest values of the catalytic constants for enzymatic hydrolysis of all known substrates for penicillin acylase: 237, 148 and 134 s-1; the corresponding Km values are 3.7 10(-5), 6.8 10(-4) and 6.2 10(-4) M at pH 7.0. The kinetics of enzymatic hydrolysis of 1-(N-phenylacetamino)-ethylphosphonic acid was investigated up to high degrees of conversion. The inhibition of penicillin acylase by high concentrations of the R-form of the substrate (with substrate inhibition constant of 0.07 M) and competitive inhibition by the reaction product, phenylacetic acid (Ki = 3.5 10(-5) M), was observed.

Aminoethylphosphonic Acid↗
PubMed1978

2-Aminoethylphosphonic acid as an indicator of Tetrahymena pyriformis W growth in protein-quality evaluation assay.

1. The concentration of 2-aminoethylphosphonic acid (AEP) in 96 h cultures of Tetrahymena pyriformis W was studied in order to apply it as an indicator in the assay of the relative nutritive value (RNV; protozoa population with test protein:protozoa population with whole-egg powder) of protein. Foodstuffs and food mixtures of different protein contents and qualities were used as test samples. 2. RNV values based on AEP determination (RNVAEP) were compared with corresponding values calculated from protozoa counts (RNVpc), as well as with biological value (BV) and net protein utilization (NPU) of the same proteins assayed on rats. 3. Both for foodstuffs and food mixtures highly significant correlations were found between RNVAEP and RNVpc, RNVAEP and both BV and NPU, and RNVpc and both BV and NPU. 4. AEP content in the protozoal suspension was preferred to cell count as a measure of growth response, since it took into account large differences in cell dimensions that were observed between cultures grown with different test proteins.

Aminoethylphosphonic Acid↗
PubMed1987

Metabolism of 2-aminoethylphosphonic acid during embryonic development of the schistosomal vector Biomphalaria glabrata.

1. Egg masses of the Planorbid snail Biomphalaria glabrata contain 2-aminoethylphosphonic acid (AEP) in three different chemical environments, as determined by 31P nuclear magnetic resonance spectroscopy, giving signals at 20.9, 21.0 and 23.4 delta. 2. The signal at 21.0 delta decreased in intensity during embryonic development, whereas the other two did not change significantly. 3. The following relationship is suggested: Extraembryonic AEP--------Intraembryonic AEP--------Phosphates. 4. pH Titration behavior of macromolecularly-bound AEP and synthetic derivatives of AEP was examined and indicates that AEP is found in the egg masses linked to other molecules in the following ways: (a) R2-NH-CH2CH2-P(O)(OH)(OR1), (b) R3-NH-CH2-P(O)(OR2)(OR1), (c) NH2-CH2CH2P(O)(OH)(OR1).

Aminoethylphosphonic Acid↗
PubMed1996

2-aminoethylphosphonic acid: biodistribution of a naturally occurring phosphonate after labelling with technetium-99m.

Phosphonic acid derivatives (P-C-P bond) are thought to be devoid of a mammalian synthetic pathway. Nevertheless, a natural phosphonate derivative, 2-aminoethylphosphonic acid (2-AEP), has been detected in animal and human tissue. After labelling with 99Tcm, biodistribution studies were performed in normal and tumour-bearing rats. A scintigraphic rabbit investigation was also completed. When expressed as percent injected dose per gram, the lung, liver, kidney and bone concentrated > 1% of the 99Tcm-2-AEP at 5 min. By 6 h, the liver, bone, marrow and kidney dominated. The 2 h rabbit scintigraphic image coincided with the rat data. Tumour-to-organ ratios showed values intermediate with those obtained with 99Tcm-diphosphonate and 99Tcm-pertechnetate. 99Tcm-2-AEP may show promise as a soft tumour scintigraphic agent because of its unique structure and low gastrointestinal uptake, provided the relatively short t1/2p of 99Tcm proves to be suitable.

Aminoethylphosphonic Acid↗