A Rapid Formaldehyde Assay Using Purpald Reagent: Application under Periodation Conditions

Quesenberry, Michael S.; Lee, Y.C.

doi:10.1006/abio.1996.0048

Cited by 98 publications

(67 citation statements)

References 2 publications

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“…After heating at 80°C for 15 min, the tryptic peptides was added with yolk sialyl glycopeptide (250 pmol) as an internal standard. The mixture was mixed with NaIO 4 (final concentration: 30 mM), and reacted at 0°C for 60 min (35)(36)(37). The oxidized glycopeptides mixture was added with Affi-Gel Hz resin (wet vol.…”

Section: Methodsmentioning

confidence: 99%

Sialic Acid-focused Quantitative Mouse Serum Glycoproteomics by Multiple Reaction Monitoring Assay

Kurogochi

Matsushista

Amano

et al. 2010

Molecular & Cellular Proteomics

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Clinical proteomics focusing on the identification and validation of biomarkers and the discovery of proteins as therapeutic targets is an emerging and highly important area of proteomics. Biomarkers are measurable indicators of a specific biological state (particularly one relevant to the risk of contraction) and the presence or the stage of disease, and are thus expected to be useful for the prediction, detection, and diagnosis of disease as well as to follow the efficacy, toxicology, and side effects of drug treatment, and to provide new functional insights into biological processes.At present, proteomics methods based on mass spectrometry (MS) have emerged as the preferred strategy for discovery of diagnostic, prognostic, and therapeutic protein biomarkers. Most biomarker discovery studies use unbiased, "identified-based" approaches that rely on high performance mass spectrometers and extensive sample processing. Semiquantitative comparisons of protein relative abundance between disease and control patient samples are used to identify proteins that are differentially expressed and, thus, to populate lists of potential biomarkers. De novo proteomics discovery experiments often result in tens to hundreds of candidate biomarkers that must be subsequently verified in serum. However, despite the large numbers of putative biomarkers, only a small number of them are passed through the development and validation process into clinical practice, and their rate of introduction is declining. The first non-standard abbreviation (MS above is standard) must be footnoted the same as the abbreviation footnote, and MRM must be the first abbreviation in the list because it is the one footnoted. After that the order does not matter.Targeted proteomics using multiple reaction monitoring (MRM) 1 is emerging as a technology that complements the discovery capabilities of shotgun strategies as well as an alternative powerful novel MS-based approach to measure a series of candidate biomarkers (1-7). Therefore, MRM is expected to provide a powerful high throughput platform for biomarker validation, although clinical validation of novel biomarkers has been traditionally relying on immunoassays (8, 9). MRM exploits the unique capabilities of triple quadrupoles (QQQ) MS for quantitative analysis. In MRM, the first and the third quadrupoles act as filters to specifically select predefined m/z values corresponding to the peptide precursor ion and specific fragment ion of the peptide, whereas the second quadrupole serves as collision cell. Several such transitions (precursor/fragment ion pairs) are monitored over time, yielding a set of chromatographic traces with retention time and signal intensity for a specific transition as coordinates. These measurements have been multiplexed to provide 30 or From the

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Section: Methodsmentioning

confidence: 99%

Sialic Acid-focused Quantitative Mouse Serum Glycoproteomics by Multiple Reaction Monitoring Assay

Kurogochi

Matsushista

Amano

et al. 2010

Molecular & Cellular Proteomics

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“…The amount of aldehyde groups generated by oxidation of the sugars was evaluated using the reaction of aldehydes with Purpald (4-amino-3-hydrazino-5-mercapto-1,2,4-triazole,4-amino-5-hydrazino-4H-1,2,4-triazole-3-thiol), described by Quesenberry and Lee (41). Blocking of CHO groups was performed by reacting avidin with 50 -200 mM semicarbazide (Sigma).…”

Section: Methodsmentioning

confidence: 99%

Biochemical and Biological Characterization of a New Oxidized Avidin with Enhanced Tissue Binding Properties

Verdoliva¹,

Bellofiore²,

Rivieccio³

et al. 2010

Journal of Biological Chemistry

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Chicken avidin and bacterial streptavidin are widely employed in vitro for their capacity to bind biotin, but their pharmacokinetics and immunological properties are not always optimal, thereby limiting their use in medical treatments. Here we investigate the biochemical and biological properties of a new modified avidin, obtained by ligand-assisted sodium periodate oxidation of avidin. This method allows protection of biotin-binding sites of avidin from inactivation caused by the oxidation step and delay of avidin clearance from injected tissue by generation of aldehyde groups from avidin carbohydrate moieties. Oxidized avidin shows spectroscopic properties similar to that of native avidin, indicating that tryptophan residues are spared from oxidation damage. In strict agreement with these results, circular dichroism and isothermal titration calorimetry analyses confirm that the ligand-assisted oxidation preserves the avidin protein structure and its biotin binding capacity. In vitro cell binding and in vivo tissue residence experiments demonstrate that aldehyde groups provide oxidized avidin the property to bind cellular and interstitial protein amino groups through Schiff's base formation, resulting in a tissue half-life of 2 weeks, compared with 2 h of native avidin. In addition, the efficient uptake of the intravenously injected 111 In-Biotin-DOTA (ST2210) in the site previously treated with modified avidin underlines that tissue-bound oxidized avidin retains its biotin binding capacity in vivo. The results presented here indicate that oxidized avidin could be employed to create a stable artificial receptor in diseased tissues for the targeting of biotinylated therapeutics.

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“…In addition, a colorimetric assay that used Purpald reagent (SigmaAldrich, St. Louis, MO) was used for detecting aldehydes in bacterium-free medium (13). Analysis of volatile fatty acids, 2-chloroacetic acid, 2HEAA, and chloride was performed with an ion chromatograph (Dionex Co., Sunnyvale, CA) using U.S. EPA method 9056A.…”

Section: Methodsmentioning

confidence: 99%

Biodegradation of Bis(2-Chloroethyl) Ether by Xanthobacter sp. Strain ENV481

McClay¹,

Schaefer²,

Vainberg³

et al. 2007

Appl Environ Microbiol

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Degradation of bis(2-chloroethyl) ether (BCEE) was observed to occur in two bacterial strains. Strain ENV481, a Xanthobacter sp. strain, was isolated by enrichment culturing of samples from a Superfund site located in the northeastern United States. The strain was able to grow on BCEE or 2-chloroethylethyl ether as the sole source of carbon and energy. BCEE degradation in strain ENV481 was facilitated by sequential dehalogenation reactions resulting in the formation of 2-(2-chloroethoxy)ethanol and diethylene glycol (DEG), respectively. 2-Hydroxyethoxyacetic acid was detected as a product of DEG catabolism by the strain. Degradation of BCEE by strain ENV481 was independent of oxygen, and the strain was not able to grow on a mixture of benzene, ethylbenzene, toluene, and xylenes, other prevalent contaminants at the site. Another bacterial isolate, Pseudonocardia sp. strain ENV478 (S. Vainberg et al., Appl. Environ. Microbiol. 72:5218-5224, 2006), degraded BCEE after growth on tetrahydrofuran or propane but was not able to grow on BCEE as a sole carbon source. BCEE degradation by strain ENV478 appeared to be facilitated by a monooxygenase-mediated Odealkylation mechanism, and it resulted in the accumulation of 2-chloroacetic acid that was not readily degraded by the strain.

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A Rapid Formaldehyde Assay Using Purpald Reagent: Application under Periodation Conditions

Cited by 98 publications

References 2 publications

Sialic Acid-focused Quantitative Mouse Serum Glycoproteomics by Multiple Reaction Monitoring Assay

Sialic Acid-focused Quantitative Mouse Serum Glycoproteomics by Multiple Reaction Monitoring Assay

Biochemical and Biological Characterization of a New Oxidized Avidin with Enhanced Tissue Binding Properties

Biodegradation of Bis(2-Chloroethyl) Ether by Xanthobacter sp. Strain ENV481

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