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Biomedical subjects

A Berry

Publications and source records attributed to A Berry.

At least 217 records · Page 12Linked to original sources
PubMed1986

Urinary cytology of a canine bladder carcinoma.

This is a study of a case of transitional cell carcinoma of the urinary bladder in a dog. Clinical and radiological signs were inconclusive. The morphology of cells exfoliated from the tumour was very similar to that of cells exfoliated from transitional cell carcinomas in human patients. On the basis of this information a diagnosis was made which was confirmed at post-mortem examination. The findings in this case report demonstrate the usefulness of this technique in the diagnosis of poorly differentiated transitional cell carcinoma.

Animal Diseases↗
PubMed1986

Comparative action of glyphosate as a trigger of energy drain in eubacteria.

Escherichia coli, Bacillus subtilis, and Pseudomonas aeruginosa, each possessing a 5-enolpyruvylshikimate 3-phosphate synthase that is sensitive to inhibition by glyphosate [N-(phosphonomethyl)glycine], provide a good cross-section of organisms exemplifying the biochemical diversity of the aromatic pathway targeted by this potent antimicrobial compound. The pattern of growth inhibition, the alteration in levels of aromatic-pathway enzymes, and the accumulation of early-pathway metabolites after the addition of glyphosate were distinctive for each organism. Substantial intracellular shikimate-3-phosphate accumulated in response to glyphosate treatment in all three organisms. Both E. coli and P. aeruginosa, but not B. subtilis, accumulated near-millimolar levels of shikimate-3-phosphate in the culture medium. Intracellular backup of common-pathway precursors of shikimate-3-phosphate was substantial in B. subtilis, moderate in P. aeruginosa, and not detectable in E. coli. The full complement of aromatic amino acids prevented growth inhibition and metabolite accumulation in E. coli and P. aeruginosa where amino acid end products directly control early-pathway enzyme activity. In contrast, the initial prevention of growth inhibition in the presence of aromatic amino acids in B. subtilis was succeeded by progressively greater growth inhibition that correlated with rapid metabolite accumulation. In B. subtilis glyphosate can decrease prephenate concentrations sufficiently to uncouple the sequentially acting loops of feedback inhibition that ordinarily link end product excess to feedback inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase by prephenate. The consequential unrestrained entry is an energy-rich substrates into the aromatic pathway, even in the presence of aromatic amino acid end products, is an energy drain that potentially accounts for the inability of end products to fully reverse glyphosate inhibition in B. subtilis. Even in E. coli after glyphosate inhibition and metabolite accumulation were allowed to become fully established, a transient period where end products were capable of only partial reversal of growth inhibition occurred. The distinctive metabolism produced by dissimilation of different carbon sources also profound effects upon glyphosate sensitivity.

3-Phosphoshikimate 1-Carboxyvinyltransferase↗
PubMed1985

Enzymatic and nonenzymatic dehydration reactions of L-arogenate.

L-Arogenate, an immediate precursor of either L-tyrosine, L-phenylalanine, or both in many microorganisms and plants, may undergo two types of dehydration reactions that yield products of increased stability. Under acidic conditions, a facile aromatization attended by loss of the C-4 hydroxyl and the C-1 carboxyl moieties results in quantitative conversion to L-phenylalanine. When aromatization was largely prevented by maintaining pH in the range of 7.5-12, a second dehydration reaction occurred in which the alanyl side chain and the carboxyl group at C-1 formed a lactam ring to yield spiro-arogenate. The latter reaction occurs at 100 degrees C, roughly 50% conversion being obtained in 2 h. The product formed from L-arogenate was authentic spiro-arogenate, as demonstrated by high-performance liquid chromatography and thin-layer chromatography identification procedures. Further confirmation was obtained by 1H nuclear magnetic resonance, ultraviolet spectroscopy, and mass spectrometry. Thus far, the conversion of L-arogenate to spiro-arogenate is not known to be enzyme catalyzed. The other dehydratase reaction, however, is catalyzed in nature by an enzyme denoted arogenate dehydratase. An improved assay is described for this in which [3H]dansyl derivatives of L-arogenate (substrate) and L-phenylalanine (product) are separated by using bidimensional thin-layer chromatography. The radioactive reaction product is then quantitated. This assay was used to study partially purified arogenate dehydratase from Pseudomonas diminuta, an organism that depends upon the arogenate pathway for L-phenylalanine biosynthesis.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids, Dicarboxylic↗
PubMed1985

Evolutionary implications of features of aromatic amino acid biosynthesis in the genus Acinetobacter.

Key enzymes of aromatic amino acid biosynthesis were examined in the genus Acinetobacter. Members of this genus belong to a suprafamilial assemblage of Gram-negative bacteria (denoted Superfamily B) for which a phylogenetic tree based upon oligonucleotide cataloging of 16S rRNA exists. Since the Acinetobacter lineage diverged at an early evolutionary time from other lineages within Superfamily B, an examination of aromatic biosynthesis in members of this genus has supplied important clues for the deduction of major evolutionary events leading to the contemporary aromatic pathways that now exist within Superfamily B. Together with Escherichia coli, Pseudomonas aeruginosa and Xanthomonas campestris, four well-spaced lineages have now been studied in comprehensive detail with respect to comparative enzymological features of aromatic amino acid biosynthesis. A. calcoaceticus and A. lwoffii both possess two chorismate mutase isozymes: one a monofunctional isozyme (chorismate mutase-F), and the other (chorismate mutase-P) a component of a bifunctional P-protein (chorismate mutase-prephenate dehydratase). While both P-protein activities were feedback inhibited by L-phenylalanine, the chorismate mutase-P activity was additionally inhibited by prephenate. Likewise, chorismate mutase-F was product inhibited by prephenate. Two isozymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase were detected. The major isozyme (greater than 95%) was sensitive to feedback inhibition by L-tyrosine, whereas the minor isozyme was apparently insensitive to allosteric control. Prephenate dehydrogenase and arogenate dehydrogenase activities were both detected, but could not be chromatographically resolved. Available evidence favors the existence of a single dehydrogenase enzyme, exhibiting substrate ambiguity for prephenate and L-arogenate.(ABSTRACT TRUNCATED AT 250 WORDS)

Acinetobacter↗
PubMed1985

Phenylalanine hydroxylase and isozymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase in relationship to the phylogenetic position of Pseudomonas acidovorans (Ps. sp. ATCC 11299a).

The evolution of aromatic amino acid biosynthesis and its regulation is under study in a large assemblage of prokaryotes (Superfamily A) whose phylogenetic arrangement has been constructed on the criterion of oligonucleotide cataloging. One section of this Superfamily consists of a well defined (rRNA homology) cluster denoted as Group III pseudomonads. Pseudomonas acidovorans ATCC 11299a, a Group III member, was chosen for indepth studies of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase, the initial regulatory enzyme of aromatic biosynthesis. This strain is of particular interest for evolutionary studies of aromatic metabolism because it possesses phenylalanine hydroxylase, an enzyme whose physiological role and distribution among prokaryotes is largely unknown. Although P. acidovorans ATCC 11299a has been of uncertain identity, we now establish it unambiguously as a species of acidovorans by virtue of its 87% DNA homology with P. acidovorans ATCC 15668 (type strain). This result conformed with enzyme patterning studies which placed ATCC 11299a into pseudomonad Group IIIa, a subgroup containing the acidovorans species. Crude extracts of Group III pseudomonads had previously been shown to share, as a common group characteristic, sensitivity of DAHP synthase to feedback inhibition by either L-tyrosine or L-phenylalanine. Detailed studies with partially purified preparations from strain ATCC 11299a revealed the presence of two distinct regulatory isozymes, DAHP synthase-phe and DAHP synthase-tyr. DAHP synthase-tyr is tightly controlled by L-tyrosine with 50% inhibition of activity being achieved at 4.0 microM effector. DAHP synthase-phe is inhibited 50% by 40 microM L-phenylalanine and exhibits dramatic changes in levels of activity, as well as chromatographic elution patterns, in response to dithiothreitol.(ABSTRACT TRUNCATED AT 250 WORDS)

3-Deoxy-7-Phosphoheptulonate Synthase↗
PubMed1985

Interconvertible molecular-weight forms of the bifunctional chorismate mutase-prephenate dehydratase from Acinetobacter calcoaceticus.

Acinetobacter calcoaceticus belongs to a large phylogenetic cluster of gram-negative procaryotes that all utilize a bifunctional P-protein (chorismate mutase-prephenate dehydratase) [EC 5.4.99.5-4.2.1.51] for phenylalanine biosynthesis. These two enzyme activities from Ac. calcoaceticus were inseparable by gel-filtration or DEAE-cellulose chromatography. The molecular weight of the P-protein in the absence of effectors was 65,000. In the presence of L-tyrosine (dehydratase activator) or L-phenylalanine (inhibitor of both P-protein activities), the molecular weight increased to 122,000. Maximal activation (23-fold) of prephenate dehydratase was achieved at 0.85 mM L-tyrosine. Under these conditions, dehydratase activity exhibited a hysteretic response to increasing protein concentration. Substrate saturation curves for prephenate dehydratase were hyperbolic at L-tyrosine concentrations sufficient to give maximal activation (yielding a Km,app of 0.52 mM for prephenate), whereas at lower L-tyrosine concentrations the curves were sigmoidal. Dehydratase activity was inhibited by L-phenylalanine, and exhibited cooperative interactions for inhibitor binding. A Hill plot yielded an n' value of 3.1. Double-reciprocal plots of substrate saturation data obtained in the presence of L-phenylalanine indicated cooperative interactions for prephenate in the presence of inhibitor. The n values obtained were 1.4 and 3.0 in the absence or presence of 0.3 mM L-phenylalanine, respectively. The hysteretic response of chorismate mutase activity to increasing enzyme concentration was less dramatic than that of prephenate dehydratase. A Km,app for chorismate of 0.63 mM was obtained. L-Tyrosine did not affect chorismate mutase activity, but mutase activity was inhibited both by L-phenylalanine and by prephenate. Interpretations are given about the physiological significance of the overall pattern of allosteric control of the P-protein, and the relationship between this control and the effector-induced molecular-weight transitions. The properties of the P-protein in Acinetobacter are considered within the context of the ubiquity of the P-protein within the phylogenetic cluster to which this genus belongs.

Acinetobacter↗
PubMed1985

The effect of null C4 alleles on complement function.

C4 is encoded at two polymorphic genetic loci (C4A and B), and "null" or unexpressed alleles are relatively common. An increased frequency of nulls has been reported in a variety of diseases. In the present study, C4 allotypes and C4 hemolytic efficiencies (the ratios of functional to antigenic levels) were determined for a population of 75 normal unrelated individuals. Of these, 28 had three gene products (single null at C4A or B) while three had no expressed C4A products and three had no C4B products (homozygous null). Mean antigenic C4 levels correlated with the number of expressed gene products but there was a wide spread of individual values. Those homozygous null for C4A had greater, and for C4B less, hemolytic efficiency than those with four gene products. However, there was no difference in the in vitro kinetics of C3 convertase formation between homozygous null C4A or C4B individuals. Therefore, the presence of null genes for C4 does not appear to compromise complement function sufficiently to account for the reported disease associations. Some of the associations may result from the fact that null genes for C4, as part of an extended HLA haplotype, may be genetically linked to disease susceptibility.

Adult↗
PubMed1983

A pair of regulatory isozymes for 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase is conserved within group I pseudomonads.

Two closely related subgroups of group I pseudomonads, which differ from one another in the overall enzymatic makeup of aromatic amino acid biosynthesis, possess in common the recently characterized major (tyrosine-sensitive) and minor (tryptophan-sensitive) isozymes of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Pseudomonas aeruginosa (17). Since these characterizations were made for strains whose phylogenetic positions have been determined by oligonucleotide cataloging, an initial perception of the evolution of aromatic pathway construction and regulation is emerging.

3-Deoxy-7-Phosphoheptulonate Synthase↗
PubMed1983

A new endotracheal tube for neonatal use.

A new endotracheal tube for neonatal use is described in which a 5FG pressure measuring catheter is attached to the convex surface of a conventional polyvinylchloride endotracheal tube. Using this modified endotracheal tube intratracheal pressure can be measured. Preliminary studies were undertaken in three infants. It was found that at high ventilatory rates (above 80/min) pressures measured within the trachea were different from those measured in the ventilator circuit.

Humans↗
PubMed1981

Mechanism of action of porphobilinogen deaminase. The participation of stable enzyme substrate covalent intermediates between porphobilinogen and the porphobilinogen deaminase from Rhodopseudomonas spheroides.

Highly stable labelled complexes are formed between porphobilinogen deaminase and stoicheiometric amounts of [14C]porphobilinogen. On completion of the catalytic cycle by the addition of excess of substrate, the complexes yield labelled product and display all the properties expected from covalently bound enzyme intermediates involved in the deaminase catalytic sequence.

Ammonia-Lyases↗
PubMed1980

Evidence that associated soil bacteria may influence root hair infection of actinorhizal plants by Frankia.

Nodulation of actinorhizal plants (Alnus rubra Bong, and others) by isolated Frankia strains occurred either at a low frequency or not at all under axenic conditions. But nodulation was achieved under nonsterile conditions and four strains of bacteria were isolated which promoted nodulation when plants were inoculated with the bacteria plus Frankia. Four strains of Pseudomonas cepacia also promoted nodulation. Root hair deformation occurred when roots of A. rubra were inoculated with these bacterial isolates, or with the bacteria plus Frankia, but rarely or not at all when roots were inoculated with the actinomycete alone. The nonendophytic bacterial strains were not detected within the nodule tissue. It is proposed that the bacterial isolates aid in the infection process at the host root hair surface, by causing root hair deformation; this may allow intimate contact between the Frankia filament and the hair wall.

Actinomycetales↗
PubMed1980

Gastric function.

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Anesthesia, Inhalation↗
PubMed1975

The importance and accuracy of the water drinking test and tonography.

The water drinking test was performed on 122 glaucoma suspect patients using the standardized Schiotz tonometer and Goldmann applanation tonometer. Additionally, the tonography was performed on 12 glaucoma suspect patients before the water test and on 69 glaucoma suspect patients after the water test. Our results showed that the most accurate test is the applanation water test. However, the accuracy of tonography was also increased if the tonography was performed after the water drinking test. The evaluation of the water drinking test only by Schiotz tonometer was not satisfactory. By using the applanation tonometry the sensitivity of the water test could be improved by 70%.

Drinking↗