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Cysteine methionine

PelZ is a hydrophilic protein of 420 amino acids with a short hydrophobic sequence at its N-terminal end which has Ae characteristics of the signal sequences of exported proteins. The signal peptide may be 24 amino acids long, which would corroborate wiA the usual length encountered in prokaryotes. The molecular cloning of the pelZ gene in an expression vector pT7-6 allowed for the specific 35S-cysteine-methionine raAo-labelling of PelZ in E. coli K38. We could detect, in crude extracts, the presence of a precursor and a mature form of PelZ. After cell fractionation, Ae mature form of PelZ could be localized in Ae periplasm of E. coli. So PelZ appears to be a protein exported by Ae Sec-dependent system of translocation. [Pg.833]

The second important issue related to commercial use of desulfurization biocatalysts is their inhibition by sulfate. The sulfur repression mechanism in most Rhodococcus species limits their use or activity in presence of sulfate- and sulfur-containing amino-acids such as cysteine, methionine, etc. To alleviate this problem, expression of the dsz genes under the control of alternate promoters has been investigated. [Pg.109]

Besada [12] described a spectrophotometric method for determination of penicillamine by reaction with nitrite and Co(II). Penicillamine is first treated with 1 M NaN02 (to convert the amino-group into a hydroxy-group), then with 0.1 M CoCl2, and finally the absorbance of the brownish-yellow complex obtained is measured at 250 nm. The process is carried out in 50% aqueous ethanol, and the pH is adjusted to 5.4— 6.5 for maximum absorbance. The calibration graph is linear over the concentration range of 0.25-2.5 mg per 50 mL, and the mean recovery (n = 3) of added drug is 99.7%. Cystine, cysteine, methionine, and other amino adds do not interfere. [Pg.135]

A particular interest for clinical applications was a possibility for detection of dopamine by its oxidation on nickel [19], cobalt [65], and osmium [66] hexacyanofer-ates. Except for oxidation of dopamine, cobalt and osmium hexacyanoferrates were active in oxidation of epinephrine and norepinephrine. For clinical analysis it is also important to carry out the detection of morphine on cobalt [67] and ferric [68] hexacyanoferrates, as well as the detection of oxidizable amino acids (cystein, methionine) by manganous [69] and ruthenium [70] hexacyanoferrate-modified electrodes. In general, oxidation of thiols was first shown for Prussian blue [71] and nickel hexacyanoferrate [72], This approach has been used for the detection of thiols in rat striatum microdialysate [73], Alternatively, the detection of thiocholine with Prussian blue was employed for pesticide determination in acetylcholine-esterase test [74],... [Pg.440]

An increase in sensitivity is realized by silver-staining, where residues containing sulfur (cysteine, methionine) or basic side chains (arginine, lysine, histidine) reduce Ag+, leading to brown or black colored bands. Here, down to 0.1 ng of protein can be detected. [Pg.77]

Husek P, Matucha P, Vrankova A, Simek P. 2003. Simple plasma work-up for a fast chromatographic analysis of homocysteine, cysteine, methionine and aromatic amino acids. J Chromatogr B 789 311. [Pg.14]

B. Sulfur-containing amino acids Cysteine Methionine... [Pg.598]

The oxidation of cysteine, as well as other amino acids, was studied by Mudd et a/. Individual amino acids in aqueous solution were exposed to ozone the reported order of susceptibility was cysteine, methionine, tryptophan, tyrosine, histidine, cystine, and phenylalanine. Other amino acids were not affected. This order is similar to that for the relative susceptibility of amino acrids to radiation and to lipid peroxides. Evaluation of the ozonization products revealed that cysteine was converted to cysteic acid, as well as cystine methionine to methionine sulfoxide tryptophan to a variety of pioducrts, including kynurenine and N-formylkynurenine tyrosine also to a variety of products, includiitg dihydroxyphenylalanine histidine to ammonia, proline, and other compounds and cystine in part to cysteic acid. In some cases, the rate and end products depended on the pH of the solution. [Pg.350]

Lugli, J. Gaziola, S.A. Azevedo, R.A. Effects of calcium, S-adenosylmethio-nine, S-(2-aminoethyl)-L-cysteine, methionine, valine and salt concentration on rice aspartate kinase isoenzymes. Plant Sci., 150, 51-58 (2000)... [Pg.331]

Cysteine Methionine S-Adenosylmethionine synthase a-Methyltransferase S-Adenosylhomocysteinase Cystathionine- /3-synthase Cystathionine- y- lyase... [Pg.515]

All amino-acid residues of proteins are potential targets for attack by reactive oxygen species (ROS) produced in the radiolysis of water however, in only a few cases have the oxidation products been fully characterized. Moreover, under most physiological conditions, cysteine, methionine, arginine, lysine, proline, histidine, and the aromatic amino acids are primary targets for ROS-mediated oxidation. [Pg.185]

In Figure 1 the equilibrium spatial structures of adsorption complexes of sulfur-containing amino acids cysteine, methionine, homocysteine and cystine on a silica surface obtained from gas phase are shown. [Pg.317]

The major nutraceutical application of marine-derived bioactive peptides has been ACE inhibition, and a partial list of identified bioactive peptides is given in Table 27.1. Fish protein has been reported to be an advantageous starting material for preparation of ACE inhibitory peptide hydrolysates (Curtis et al., 2002). Marine-derived protein hydrolysate tends to contain high concentrations of cysteine, methionine, and arginine, all of which help reduce hypertension (Kristinsson, 2007). Such marine-derived peptides could be used as potent functional food additives and represent a healthier and natural alternative to ACE inhibitor drugs (Li et aL, 2004). Currently, the bioactive oligopeptides from dried bonito and sardine muscle have been approved as Foods for Specified Health Use by the Ministry of Health and Welfare in Japan. [Pg.500]

Free amino acids readily form chloramines in reactions with HOC1. However, the reaction can be postponed by the presence of amino acids whose side groups have reducing properties (as is the case with cysteine, methionine, and tryptophan). Amino acid chloramines located at the a-carbon are unstable, decomposing by deamination and decarboxylation. The final stable products are ammonia, chloride, and the aldehyde respective to the amino acid carbon backbone (H12, Z4) ... [Pg.180]


See other pages where Cysteine methionine is mentioned: [Pg.84]    [Pg.363]    [Pg.221]    [Pg.358]    [Pg.404]    [Pg.1073]    [Pg.87]    [Pg.153]    [Pg.549]    [Pg.190]    [Pg.205]    [Pg.299]    [Pg.403]    [Pg.77]    [Pg.97]    [Pg.262]    [Pg.263]    [Pg.199]    [Pg.220]    [Pg.1154]    [Pg.193]    [Pg.195]    [Pg.195]    [Pg.7]    [Pg.364]    [Pg.114]    [Pg.342]    [Pg.570]    [Pg.135]    [Pg.153]    [Pg.130]    [Pg.291]    [Pg.153]    [Pg.344]    [Pg.176]   
See also in sourсe #XX -- [ Pg.141 ]




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Cysteine conversion from methionine

Cysteine methionine relationship

Cysteine methionine sparing

Methionine cysteine and

Modification of Methionine and Cysteine

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