ARGININE DEGRADATION BYMICROCOCCUS PYOGENESVAR.AUREUS

1955 ◽  
Vol 1 (5) ◽  
pp. 339-345 ◽  
Author(s):  
Albert W. Jackson ◽  
Arthur E. Pasieka

Whereas intact cells of a number of strains of M. pyogenes var. aureus rapidly degrade arginine to ornithine with no observable accumulation of citrulline, the latter amino acid is almost the sole ninhydrin-positive product of arginine degradation by acetone-dried cells of this species. Recovery of the products of arginine degradation shows that arginine is degraded to ornithine by intact cells with the liberation of two moles of ammonia and one of carbon dioxide and to citrulline by acetone-dried cells with the liberation of ammonia. It is concluded from the above observations that degradation of arginine to ornithine by M. pyogenes var. aureus proceeds via citrulline. Maximum activity of arginine-desimidase was observed at pH 6.5 and the quantity of enzyme within the cells was found to depend on the arginine concentration of the growth medium, with maximum enzyme formation at about 100 γ/ml. of arginine.

1972 ◽  
Vol 50 (12) ◽  
pp. 2535-2543 ◽  
Author(s):  
B. R. Grant ◽  
F. Winkenbach ◽  
D. T. Canvin ◽  
R. G. S. Bidwell

The effects of nitrate, nitrite, and ammonia were compared using chloroplasts prepared from Acetabularia mediterranea and spinach and intact cells of Acetabularia and Dunaliella tertiolecta. Nitrate was without effect in all systems. Spinach chloroplasts were strongly inhibited by nitrite at 5 mM, Acetabularia cells were somewhat inhibited, but Dunaliella cells and chloroplast preparations from Acetabularia were unaffected. Ammonia at 5 mM inhibited spinach and Acetabularia chloroplasts, but its effect on the other systems was slight. It decreased oxygen production in chloroplasts and Dunaliella cells, but did not affect carbon dioxide fixation.These results are interpreted on the basis of varying rates of uptake, metabolism, and detoxification of the ions in different preparations. Whole cells and Acetabularia chloroplast preparations make amino acids, but spinach chloroplasts do not. This accounts for the greater sensitivity of the latter, and for the decreased oxygen production in the presence of ammonia in whole cells, which is presumably caused by increased respiration accompanying amino acid formation. The insensitivity of the Acetabularia chloroplast preparation is attributed to the properties of the membrane, apparently derived from tonoplast fragments, which surrounded the small cytoplasmic droplets present in these preparations.


Science ◽  
1995 ◽  
Vol 268 (5209) ◽  
pp. 439-442 ◽  
Author(s):  
M. Nowak ◽  
P. Kearney ◽  
Sampson ◽  
M. Saks ◽  
C. Labarca ◽  
...  

2010 ◽  
Vol 4 (5) ◽  
pp. 771-775 ◽  
Author(s):  
Ugochukwu E. Aronu ◽  
Hallvard F. Svendsen ◽  
Karl Anders Hoff

1998 ◽  
Vol 66 (6) ◽  
pp. 2576-2586 ◽  
Author(s):  
Leigh Rice Washburn ◽  
Keith E. Weaver ◽  
Elizabeth J. Weaver ◽  
Wendy Donelan ◽  
Suhaila Al-Sheboul

Earlier studies implied a role for Mycoplasma arthritidis surface protein MAA2 in cytadherence and virulence and showed that it exhibited both size and phase variability. Here we report the further analysis of MAA2 and the cloning and sequencing of the maa2 gene from two M. arthritidis strains, 158p10p9 and H606, expressing two size variants of MAA2. Triton X-114 partitioning and metabolic labeling with [3H]palmitic acid suggested lipid modification of MAA2. Surface exposure of the C terminus was indicated by cleavage of monoclonal antibody-specific epitopes from intact cells by carboxypeptidase Y. The maa2genes from both strains were highly conserved, consisting largely of six (for 158p10p9) or five (for H606) nearly identical, 264-bp tandem direct repeats. The deduced amino acid sequence predicted a largely hydrophilic, highly basic protein with a 29-amino-acid lipoprotein signal peptide. The maa2 gene was expressed inEscherichia coli from the lacZ promoter of vector pGEM-T. The recombinant product was approximately 3 kDa larger than the native protein, suggesting that the signal peptide was not processed in E. coli. The maa2 gene and upstream DNA sequences were cloned from M. arthritidisclonal variants differing in MAA2 expression state. Expression state correlated with the length of a poly(T) tract just upstream of a putative −10 box. Full-sized recombinant MAA2 was expressed inE. coli from genes derived from both ON and OFF expression variants, indicating that control of expression did not include alterations within the coding region.


1961 ◽  
Vol 39 (11) ◽  
pp. 1717-1735 ◽  
Author(s):  
P. G. Scholefield

The cumulative entry of amino acids into Ehrlich ascites carcinoma cells is due to the presence of active transport systems, each with its own specific range of substrates. Several amino acids and amino acid analogues may have an affinity for the same transport system and thus may inhibit transport of other amino acids by acting as competitive inhibitors or competitive substrates. Loss of methionine from ascites cells takes place by a diffusion process which obeys Fick's law. Leucine accumulation by ascites cells is small and is increased on addition of certain other amino acids. The increase is not due to inhibition of leucine oxidation as increase in the rate of production of radioactive carbon dioxide from labeled leucine also occurs. Kinetic aspects of these results are discussed.


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