Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: CAS:1069-31-4 (ornithine)
6,755 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Escherichia coli [3H]DNA supplied to vegetative cultures of wild-type (mt+) and CW15 (mt+;mutant lacking the cell wall) Chlamydomonas reinhardi could bind to the cell wall of the wild-type and to the cell membrane of CW15 mutant cells. The extent of this binding decreased with time and was to a large degree (over 90%) DNA-ase-sensitive. Nevertheless, about 0.01% of the bacterial DNA remained irreversibly associated with the cells when they reached stationary phase. The irreversible binding of the donor bacterial DNA to Chlamydomonas cells could be increased by treatment of the cultures with polycations such as DEAE-dextran, poly-L-lysine and poly-L-ornithine. Although the CW15 cells rapidly degraded bacterial DNA in the culture medium wild-type cells showed only a small effect on the molecular weight of the donor DNA. The acid-insoluble radioactivity irreversibly bound to WT (+) cells consisted mainly of oligonucleotides with a small proportion present as less depolymerized donor DNA. No radioactivity, however, was found to be associated with the recipient high molecular weight Chlamydomonas DNA. No labeled donor DNA could be recognized in the cells given bacterial [3H]DNA in early stationary phase. Instead, radioactivity found in Chlamydomonas DNA corresponded to reutilization of [3H]thymine derivatives released as a result of [3H]DNA degradation. No evidence for the integration of detectable amounts of donor DNA sequences into the host cell DNA was obtained.
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PMID:Uptake of bacterial DNA by Chlamydomonas reinhardi. 80 41

4-Aminobutyrate aminotransferase (GABAT) from Pseudomonas aeruginosa was purified 64-fold to apparent electrophoretic homogeneity from cells grown with 4-aminobutyrate as the only source of carbon and nitrogen. Purified GABAT catalyzed the transamination of 4-aminobutyrate, N2-acetyl-L-ornithine, L-ornithine, putrescine, L-lysine, and cadaverine with 2-oxoglutarate (listed in order of decreasing activity). The enzyme is induced in cells grown on 4-guanidinobutyrate, 4-aminobutyrate, or putrescine as the only carbon and nitrogen source. Cells grown on arginine or on glutamate contained low levels of the enzyme. The regulation of the synthesis of GABAT as well as the properties of the mutant with an inactive N2-acetyl-L-ornithin 5-aminotransferase suggest that GABAT functions in the biosynthesis of arginine by convertine N2-acetyl-L-glutamate 5-semialdehyde to N2-acetyl-Lornithine as well as in catabolic reactions during growth on putrescine or 4-guanidinobutyrate but not during growth on arginine.
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PMID:Role of 4-aminobutyrate aminotransferase in the arginine metabolism of Pseudomonas aeruginosa. 82 9

The specificity of amino acid transport in normal (high-glutathione) sheep erythrocytes was investigated by studying the interaction of various neutral and dibasic amino acids in both competition and exchange experiments. Apparent Ki values were obtained for amino acids as inhibitors of L-alanine influx. Amino acids previously found to be transported by high-glutathione cells at fast rates (L-cysteine, L-alpha-amino-n-butyrate) were the most effective inhibitors. D-Alanine and D-alpha-amino-n-butyrate were without effect. Of the remaining amino acids studied, only L-norvaline, L-valine, L-norleucine, L-serine and L-2,4-diamino-n-butyrate significantly inhibited L-alanine uptake. L-Alanine efflux from pre-loaded cells was markedly stimulated by extracellular L-alanine. Those amino acids that inhibited L-alanine influx also stimulated L-alanine efflux. In addition, D-alanine, D-alpha-amino-n-biutyrate, L-threonine, L-asparagine, L-alpha, beta-diaminoproprionate, L-ornithine, L-lysine and S-2-aminoethyl-L-cysteine also significantly stimulated L-alanine efflux. L-Lysine uptake was inhibited by L-alanine but not by D-alanine, and the inhibitory potency of L-alanine was not influenced by the replacement of Na+ in the incubation medium with choline. L-Lysine efflux from pre-loaded cells was stimulated by L-alanine but not by D-alanine. It is concluded that these cells possess a highly selective stero-specific amino acid-transport system. Although the optimum substrates are small neutral amino acids, this system also has a significant affinity for dibasic amino acids.
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PMID:Substrate specificity of amino acid transport in sheep erythrocytes. 84 80

The uptake of cystine by vesicles prepared from rat kidney brush borders occurs by two distinct transport systems. The higher affinity system is inhibited by the dibasic amino acids lysine, arginine, and ornithine. The lower affinity system, unaffected by dibasic amino acids, appears to correspond to that observed by studying uptake of cystine by kidney slices.
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PMID:Transport interaction of cystine and dibasic amino acids in renal brush border vesicles. 87 48

Cystinuria is a disease characterized by the excessive elimination of cystine and of dibasic amino acids (lysine, arginine, and ornithine) through urine of homozygotes. This study included 6 children complaining of abdominal pain with or without hematuria. The existence of renal radio-opaque lithiasis was confirmed in 5 of them and in the sixth, it was vesical. The clinical and analytic data were practically normal with the exception of the qualitative test of the amino acid urinary excretion that showed increase in urinary excretion of cystine. Likewise, percentages of tubular reabsorption were pathological in all the patients showing values between 35.4% and 74%. The diagnosis of systini-lysinuric lithiasis was established through amino acid excretion study in the six patients which was below normal; it fluctuated between 36% and 74%. Lysine, together with cystine, was the most frequently affected.
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PMID:[Cystinolysinuric lithiasis]. 91 52

Congenital hyperdibasicaminoaciduria without cystinuria was detected in a mentally but not physically retarded boy. Plasma lysine and arginine were normal, whereas plasma ornithine was decreased. Although oral or intravenous loading tests could not be performed, the history without vomiting or diarrhea, and the normal physical development indicated an unimpaired intestinal transport of basic aminoacids. Our case could be a further mutant of this transport defect which concerns the renal tubuli only.
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PMID:[Congenital hyperlysin-arginin-ornithinuria in a mentally retarded child (author's transl)]. 91 28

Sixty-eight Haemophilus somnus strains isolated from the bovine in Canada and the U.S.A. were compared. In media enriched with 5% ovine serum, 5% bovine serum and 10% yeast extract, H. somnus fermented glucose, levulose, maltose, mannitol, mannose, sorbitol, trehalose and xylose, but failed to ferment arabinose, dulcitol, galactose, inositol, lactose, raffinose, rhamnose, salicin and sucrose. The organisms acidified litmus milk, produced cytochrome oxidase, indole and hydrogen sulfide (H(2)S) and reduced nitrates to nitrites. The motility, methyl-red, acetylmethyl-carbinol urease catalase, citrate, malonate, lysine, ornithine and arginine tests were negative. Haemophilus somnus was resistant to lincomycin, neomycin and triple sulfa, but susceptible to ampicillin, chloramphenicol, streptomycin, penicillin and tetracycline. No antigenic differences were noted between strains when tested against rabbit antisera of eight strains using agglutination, complement-fixation, immunodiffusion and counterimmunoelectrophoresis tests. Low titre cross-reactions were found in the agglutination tests with some of the anti-H. somnus rabbit sera with Actinobacillus lignieresi and Moraxella bovis. No distinct antigenic similarities to nine other species of pathogenic bacteria of animal origin were found. No difference was observed between H. somnus isolates from Ontario and those from western Canada and the U.S.A.
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PMID:A comparison of various Haemophilus somnus strains. 92 55

The peptidoglycan of Bifidobacterium globosum contains ornithine and lysine alternately in the same position of the peptide subunit. The uridine diphospho-N-acetylmuramyl-alanyl-D-glutamic acid: diamino acid ligase of this organism was purified 700-fold. Since the activities for the incorporation of ornithine and lysine into uridine diphospho-N-acetylmuramyl-tripeptide did not separate during purification and since the incorporation of ornithine is competitively inhibited by lysine and vice versa, both ornithine and lysine are assumed to be incorporated by one single enzyme. Studies on the specificity of the ligase toward analogs of ornithine have shown that the enzyme requires a diamino, monocarboxylic acid with 4-6 carbon atoms. Methylation of the epsilon-amino group or hydroxylation of the delta-carbon atom of lysine decreases the competitive properties of the analog, whereas the substitution of the gamma-methylen group by sulfur (S-2-aminoethyl cysteine) results in a highly competitive compound.
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PMID:On the specificity of the uridine diphospho-N-acetylmuramyl-alanyl-D-glutamic acid: diamino acid ligase of Bifidobacterium globosum. 93 11

1. A family is reported with an unusual type of cystinuria. 2. The propositus presented with a cystine renal stone; the renal tubular reabsorption of cystine was grossly abnormal but the tubular reabsorption of ornithine, lysine and arginine was only slightly less than normal. 3. One of the children of the propositus escreted cystine and lysine in increased amounts typical of type II heterozygotes for cystinuria. 4. The renal transport defect in this family may represent one end of the spectrum of cystinuria or it may be a form akin to isolated hypercystinuria.
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PMID:Cystinuria: a new genetic variant. 93 63

The concentration of the amino acids has been determined in granulocytes from healthy men and women by chromatographic analysis on ion-exchanging resins. Except taurine, ornithine and aspartic acid, the concentrations of all the amino acids are greater in the cells isolated from women. The most variable amino acids are alanine, valine, metionine, isoleucine, leucine, tyrosine, phenylalanine, lysine and histidine. Taurine represents 50% of the pool determined from men, whereas for women it represents only 25%.
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PMID:Quantitative determination of granulocytic amino acids in healthy men and women. 94 90


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