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Query: CAS:1069-31-4 (ornithine)
 6,755 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In enzymic preparations from mouse kidney stimulated with the anabolic steroid Durabolin (nandrolone phenpropionate) lysine and ornithine were shown to inhibit the decarboxylation of each other competitively. The Michaelis constants for the decarboxylations were approximately equal to the inhibition constants of the two amino acids. The pH optima of the decarboxylation of lysine and ornithine were found to be identical. Chromatographic studies of the enzyme preparation on a Sephadex G-150 Superfine column did not bring about a separation of the two enzyme activities. The ratio of the decarboxylating activities was practically the same during the elution. Lysine decarboxylating activity was also shown to be present in growth hormone stimulated rat liver. The results are in agreement with the assumption that the decarboxylation of lysine and ornithine is carried out by the same enzyme.
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PMID:Evidence of decarboxylation of lysine by mammalian ornithine decarboxylase. 2 Jul 36

The primary amine dehydrogenase of Pseudomonas putida NP was purified to homogeneity as judged by polyacrylamide gel electrophoresis. Cytochrome c or an artificial electron acceptor was required for amine dehydrogenase activity. The enzyme was nonspecific, readily oxidizing primary monoamines, benzylamine, and tyramine; little or no measurable activity was detected with isoamines, L-ornithine, L-lysine, and certain diamines or polyamines. The pH optima for n-butylamine, benzylamine, and n-propylamine were 7.0, 6.5, and 7.0, respectively. The molecular weight of the enzyme was 112,000 as determined by gel filtration and 95,300 as analyzed by sedimentation equilibrium. Subunit analysis by sodium dodecyl sulfate gel electrophoresis suggested that the enzyme was composed of two nonidentical subunits with molecular weights of 58,000 and 42,000. The absorption spectrum of the purified enzyme was indicative of a hemoprotein, exhibiting absorption maxima at 277, 355, and 408 nm. Reduction with sodium dithionite or amine substrates resulted in absorption maxima at 523 and 552 nm and a shift in the Soret peak to 416 nm. These results suggested that the enzyme is a hemoprotein of the type c cytochrome. There was no evidence that flavins were present.
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PMID:Purification and characterization of a heme-containing amine dehydrogenase from Pseudomonas putida. 2 67

Nitrogen control in Salmonella typhimurium is not limited to glutamine synthetase but affects, in addition, transport systems for histidine, glutamine, lysine-arginine-ornithine, and glutamate-aspartate. Synthesis of both glutamine synthetase and transport proteins is elevated by limitation of nitrogen in the growth medium or as a result of nitrogen (N)-regulatory mutations. Increases in the amounts of these proteins were demonstrated by direct measurements of their activities, by immunological techniques, and by visual inspection of cell fractions after gel electrophoresis. The N-regulatory mutations are closely linked on the chromosome to the structural gene for glutamine synthetase, glnA: we discuss the possibility that they lie in a regulatory gene, glnR, which is distinct from glnA. Increases in amino acid transport in N-regulatory mutant strains were indicated by increased activity in direct transport assays, improved growth on substrates of the transport systems, and increased sensitivity to inhibitory analogs that are trnasported by these systems. Mutations to loss of function of individual transport components (hisJ, hisP, glnH, argT) were introduced into N-regulatory mutant strains to determine the roles of these components in the phenotype and transport behavior of the strains. The structural gene for the periplasmic glutamine-binding protein, glnH, was identified, as was a gene argT that probably encodes the structure of the lysine-arginine-ornithine-binding protein. Genes encoding the structures of the histidine- and glutamine-binding proteins are not linked to glnA or to each other by P22-mediated transduction; thus, nitrogen control is exerted on several unlinked genes.
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PMID:Nitrogen control of Salmonella typhimurium: co-regulation of synthesis of glutamine synthetase and amino acid transport systems. 3 21

The effects of L-amino acids on arginase from the hepatopancreas of the snail Ariophanta (=Cryptozona) ligulata were studied. This enzyme was inhibited by ornithine, valine, lysine, leucine, isoleucine, proline and threonine. The other amino acids were without any significant effect. Only ornithine was a non-competitive inhibitor, where as all the other inhibitory amino acids were competitive.
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PMID:The inhibition of arginase from the hepatopancreas of a terrestrial snail by amino acids. 6 44

The binding of FITC-labeled poly-L-ornithine and poly-L-lysine to fresh or neuraminidase treated human, rat or rabbit erythrocytes was investigated by simultaneous cell volume and cell membrane fluorescence measurements in a flow cytometer. The cell volume was converted into cell surface and the distribution curve of the fluorescence/micrometer2 cell surface was calculated from all histogram classes by a computer program. The mean fluorescence/micrometer2 cell surface as a measure of the density of the negative charges on the cell surface was directly proportional to the elctrophoretic mobility of the erythrocytes, showing that polycation binding can effectively be used for the measurement of the electrophoretic mobility of erythrocytes. The computer fitting of the experimental two parameter histograms by two dimensional Gaussian normal distributions was found to be a very efficient way of data reduction, and a good separation of overlapping cell clusters was possible even in the case of low total numbers of cells in the histogram.
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PMID:Flow cytometry as a new method for the measurement of electrophoretic mobility of erythrocytes using membrane charge staining by fluoresceinated polycations. 8 64

Urinary excretion of albumin, free light chains of immunoglobulins and beta-2-microglobulin was measured after injection of certain amino acids and derivatives. Substances with a positively charged group located terminally in the molecule (ornithine, lysine, arginine, and the almost not metabolized epsilon-amino-caproic acid, and Cyclocaprone) proved to inhibit instantaneously the tubular protein reabsorption. Lysine is the most effective molecule tested. We hypothesize that the initial event in the normal tubular protein reabsorption is a binding between a free positive amino- or guanidino-group in the protein molecule and a negative site on the tubular cell surface. In an attempt to achieve complete inhibition of tubular protein reabsorption, large doses of lysine were injected intravenously. The maximal protein clearance rose from the exceedingly low baseline excretion to values probably representing near complete inhibition of protein reabsorption. The minimal value of albumin concentration in the glomerular filtrate was calculated to 2.6 mg/l.
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PMID:Studies on renal tubular protein reabsorption: partial and near complete inhibition by certain amino acids. 9 29

Incubation of soluble human liver arginase (L-arginine amidinohydrolase, EC 3.5.3.1) with p-hydroxymercuribenzoate resulted in the dissociation of the enzyme into active dimers. Addition of 2-mercaptoethanol resulted in the regeneration of the tetrameric enzyme. When arginase, bound covalently to nylon, was incubated with p-hydroxymercuribenzoate, matrix-bound dimers were obtained. Incubation of these species with 2-mercaptoethanol resulted in stable, unmodified dimers. Based on this dissociation of arginase, a model with D2-symmetry is suggested for this enzyme. The specific activity, the Km value for arginine, pH optimum and the inhibition constants for ornithine and lysine were determined for monomeric, dimeric and tetrameric forms. It is concluded that the behaviour of the active sites of the monomers is not substantially altered by the interaction of these species in the oligomeric molecule.
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PMID:Subunit interactions and immobilised dimers of human liver arginase. 10 58

Ornithine-, lysine- and arginine-decarboxylase activity of 218 P. multocida strains, isolated from birds of varying disease symptoms in Bulgaria and CSSR, and from pigs, rabbits and birds in Cuba, USSR and CSSR, was studied after the method of Moller. Positive ornithine decarboxylase activity was established in 211 strains, low -- in 2, and negative -- in 5 strains. Low arginine decarboxylase activity was observed in 12 Pasteurella strains, while in 14 -- low lysine decarboxylase activity. The presence of ornithine decarboxylase activity can be used, along with the cultural and biochemical properties and with lyzation by a specific bacteriophage, as a taxonomic character for the species. All Pasteurella strains pathogenic for white mice, produce ornithine-decarboxylase. Lines of the strain X 73 obtained following gamma-irradiation having lost their ornithine-decarboxylase are pathogenic for white mice.
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PMID:[Decarboxylase activity study of Pasteurella multocida]. 12 Jun 31

Plasma tryptophan (Trp) is reported to be decreased in some patients with the carcinoid syndrome. To determine if the plasma levels of other amino acids are also altered in the carcinoid syndrome, we used a fas-liquid chromatographic method to determine the plasma amino acid concentration of nine patients with the carcinoid syndrome and nine age-matched healthy control subjects. In comparison to the control subjects, the patients with the carcinoid syndrome had decreased plasma concentration of valine (Val), isoleucine (Ile), lysine (Lys), and ornithine (Orn), and an increased plasma concentration of methionine (Met). With the exception of a decrease in urinary excretion of proline (Pro) and hydroxyporline (Hyp), the patients with the carcinoid syndrome had normal quantities of amino acids in their urine. Plasma Met returned to normal when serotonin production by the tumor was reduced 60% by parachlorophenylalanine (PCPA); the other amino acid abnormalities persisted. Further studies are needed to determine the significance of these amino acid abnormalities.
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PMID:Plasma amino acids in patients with the carcinoid syndrome. 13 95

Poly L-lysine, poly L-ornithine, and histone significantly inhibited the iodide uptake by the thyroid slices, as previously reported. These basic polymers diminshed Na, K-ATPase and concomitantly markedly elevated Mg-ATPase activity in the NaI-treated microsomal preparation and the plasma membrane fraction obtained from thyroid. Poly L-glutamic acid, which was noneffetive to the iodide uptake in vitro, did not show such phenomenon. K-dependent p-nitrophenylphosphatase activity which is considered to reflect the terminal step of the reaction sequence of Na, K-ATPase was also inhibited by poly L-lysine. The effects mentioned above of poly L-lysine and other basic polyamino acids on membrane ATPase system were only found in the preparations from thyroid. The inhibitory effect of these reagents on thyroidal iodide uptake was discussed in terms of the change in membrane ATPase activities.
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PMID:Some properties of thyroidal membrane adenosinetriphosphatase and iodide uptake: effects of basic polyamino acids. 13 43


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