M53701

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Showing 1-27 of 27 results for "M53701" within Papers

Relative quantification of tau-related peptides using guanidino-labeling derivatization (GLaD) with online-LC on a hybrid ion trap (IT) time-of-flight (ToF) mass spectrometer.

Jessica Z Bereszczak et al.

Journal of the American Society for Mass Spectrometry, 18(2), 201-207 (2006-10-28)

Development of a quantification method based on isotopic variants of O-methyl isourea (OMIU) in conjunction with reversed-phase (RP) liquid chromatography (LC) electrospray mass spectrometry is described for determining the relative quantification of tau-related peptides Ac-VQIVXK-NH2. Extracted ion chromatograms of the

Jack bean urease (EC 3.5.1.5). V. On the mechanism of action of urease on urea, formamide, acetamide, N-methylurea, and related compounds.

N E Dixon et al.

Canadian journal of biochemistry, 58(12), 1335-1344 (1980-12-01)

Acetamide and N-methylurea have been shown for the first time to be substrates for jack bean urease. In the enzymatic hydrolysis of urea, formamide, acetamide, and N-methylurea at pH 7.0 and 38 degrees C, kcat has the values 5870, 85

Heat stability of milk: influence of modification of lysine and arginine on the heat stability-pH profile.

S I Shalabi et al.

The Journal of dairy research, 49(4), 607-617 (1982-11-01)

Several dicarbonyl compounds (glyoxal, substituted glyoxals, diacetyl and 1, 2-cyclohexanedione) had a marked stabilizing effect on the heat stability of milk, especially in the presence of urea. These reagents are believed to modify arginine more or less specifically suggesting an

Optimization of carbamylation conditions and study on the effects on the product ions of carbamylation and dual modification of the peptide by Q-TOF MS.

Cheng Guo et al.

European journal of mass spectrometry (Chichester, England), 24(5), 384-396 (2018-07-26)

Modified peptides fragmented by collision-induced dissociation can offer additional sequence information, which is beneficial for the de novo sequencing of peptides. Here, the model peptide VQGESNDLK was carbamylated. The optimal conditions were as follows: temperature of 90℃, pH of 7

Lysine residues, but not carbohydrates, are required for the regulatory function of H on the amplification C3 convertase of complement.

M H Jouvin et al.

Journal of immunology (Baltimore, Md. : 1950), 133(6), 3250-3254 (1984-12-01)

Lysine epsilon-amino groups of human factor H were selectively converted to guanidino groups by treatment with 0.1 M O-methylisourea at pH 10.4. Guanidination resulted in a dose-dependent decrease in the capacity of the regulatory protein to accelerate decay dissociation of

Effect of lysine modification on the conformation and indomethacin binding properties of human serum albumin.

S Tayyab et al.

International journal of biological macromolecules, 26(2-3), 173-180 (1999-10-12)

In order to study the involvement of lysine residues of human serum albumin (HSA) in the binding of indomethacin, HSA was treated with different molar excess of acetic anhydride, succinic anhydride and O-methylisourea which resulted in differently modified preparations: 30%

Increased sensitivity of tryptic peptide detection by MALDI-TOF mass spectrometry is achieved by conversion of lysine to homoarginine.

J E Hale et al.

Analytical biochemistry, 287(1), 110-117 (2000-11-18)

Mass spectrometric techniques for identification of proteins by "mass fingerprinting" (matching the masses of tryptic peptides from a protein digest to the theoretical peptides in a database) such as matrix-assisted laser desorption ionization-time of flight (MALDI-TOF) are rapidly growing in

Profiling constitutive proteolytic events in vivo.

John C Timmer et al.

The Biochemical journal, 407(1), 41-48 (2007-07-26)

Most known organisms encode proteases that are crucial for constitutive proteolytic events. In the present paper, we describe a method to define these events in proteomes from Escherichia coli to humans. The method takes advantage of specific N-terminal biotinylation of

Involvement of lysine residues in the binding of ovine chorionic somatomammotropin to lactogenic and somatotropic receptors.

N Chêne et al.

FEBS letters, 166(2), 352-356 (1984-01-30)

The biological activities of several ovine chorionic somatomammotropin (oCS) derivatives obtained by chemical modification of the lysine residues were studied by radioreceptor assays using rabbit mammary homogenates (lactogenic activity, L.A.) and liver homogenates (somatotropic activity, S.A.). Even if the control

Structure-toxicity relationships of neurotoxin RTX-III from the sea anemone Radianthus macrodactylus: modification of amino groups.

V M Mahnir et al.

Toxicon : official journal of the International Society on Toxinology, 29(7), 819-826 (1991-01-01)

The effect of modification of amino groups on RTX-III induced lethality in mice has been studied. The toxicity was not affected by guanidination of one or two lysine residues with O-methylisourea, but guanidination of three or four lysine residues decreased

The antigenic structure of HBsAg: study of the d/y subtype determinant by chemical modification and site directed mutagenesis.

E Guerrero et al.

Molecular immunology, 27(5), 435-441 (1990-05-01)

Lysine residue 122 of the major protein of HBsAg/adw has been shown previously to be involved in the d subtype determinant. We demonstrate here that the corresponding residue of the HBsAg/ayw, arginine 122, does not play such a critical role

Changes in protein stability upon chemical modification of lysine residues of bovine serum albumin by different reagents.

K M Fazili et al.

Biochemistry and molecular biology international, 31(5), 807-816 (1993-12-01)

Using acetic anhydride, potassium cyanate and O-methyl isourea six chemically modified derivatives of bovine serum albumin with chemical modification on lysine side chains have been prepared. All the modified preparations were found to be homogeneous with respect to size and

Integrating Lys-N proteolysis and N-terminal guanidination for improved fragmentation and relative quantification of singly-charged ions.

Valerie J Carabetta et al.

Journal of the American Society for Mass Spectrometry, 21(6), 1050-1060 (2010-03-09)

The study of isolated protein complexes has greatly benefited from recent advances in mass spectrometry instrumentation and quantitative, isotope labeling techniques. The comprehensive characterization of protein complex components and quantification of their relative abundance relies heavily upon maximizing protein and

Complex formation of guanidinated bovine trypsin inhibitor (Kunitz) with trypsin, chymotrypsin and trypsinogen as studied by the spin-label technique.

H R Wenzel et al.

FEBS letters, 140(1), 53-57 (1982-04-05)

Arginyl residues and thermal stability in proteins.

F S Qaw et al.

Molecular and cellular biochemistry, 71(2), 121-127 (1986-08-01)

Guanidination and amidination of bovine serum albumin, yeast enolase and yeast alcohol dehydrogenase were accompanied by increases in thermal stability at lower extents of modification. Decreases in thermal stability result from greater modification. These results support suggestions that surface guanidino

Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides.

F L Brancia et al.

Rapid communications in mass spectrometry : RCM, 14(21), 2070-2073 (2000-11-21)

Analysis of tryptic digests of proteins using matrix-assisted laser desorption/ionization (MALDI) mass spectrometry commonly results in superior detection of arginine-containing peptides compared with lysine-containing counterparts. The effect is attributable in part to the greater stability of the arginine-containing peptide ions

Guanidino labeling derivatization strategy for global characterization of peptide mixtures by liquid chromatography matrix-assisted laser desorption/ionization mass spectrometry.

Francesco L Brancia et al.

Analytical chemistry, 76(10), 2748-2755 (2004-05-18)

Guanidination performed with isotopic isoforms of O-methylisourea was used in combination with reversed-phase liquid chromatography (LC) matrix-assisted laser desorption/ionization to characterize, both qualitatively and quantitatively, protein mixtures. Synthesis of (13)C- and (15)N(2)-labeled O-methylisourea sulfate produces a molecule that is 3

Tissue-specific signatures in tick cell line MS profiles.

Dmitry S Loginov et al.

Parasites & vectors, 12(1), 212-212 (2019-05-08)

The availability of tick in vitro cell culture systems has facilitated many aspects of tick research, including proteomics. However, certain cell lines have shown a tissue-specific response to infection. Thus, a more thorough characterization of tick cell lines is necessary.

Chemical modulation of the chaperone function of human alphaA-crystallin.

Ashis Biswas et al.

Journal of biochemistry, 144(1), 21-32 (2008-03-18)

alphaA-crystallin is abundant in the lens of the eye and acts as a molecular chaperone by preventing aggregation of denaturing proteins. We previously found that chemical modification of the guanidino group of selected arginine residues by a metabolic alpha-dicarbonyl compound

The selectivity of amino acid and peptide amidination with O-methylisourea.

H Wojciechowska et al.

Acta biochimica Polonica, 29(3-4), 197-204 (1982-01-01)

Selectivity of amidination using ornithine as model amino acid was investigated in detail. The results obtained were taken advantage of for studying the reactions with other polyfunctional amino acids: beta-tyrosine, isoserine, 2,3-diaminopropionic acid, 2,6-diamino-7-hydroxyazelaic acid and with the pentapeptide amide

Approach for determining protein ubiquitination sites by MALDI-TOF mass spectrometry.

Dongxia Wang et al.

Analytical chemistry, 77(5), 1458-1466 (2005-03-01)

Protein ubiquitination plays an important role in the degradation and other functional regulation of cellular proteins in organisms ranging from yeasts to mammals. Trypsin digestion of ubiquitin conjugated proteins produces diglycine branched peptides in which the C-terminal Gly-Gly fragment of

Chemical modification of bovine pancreatic trypsin inhibitor for single site coupling of immunogenic peptides for NMR conformational analysis.

S Ebina et al.

The Journal of biological chemistry, 264(14), 7882-7888 (1989-05-15)

Procedures for chemical modification of bovine pancreatic trypsin inhibitor (BPTI) to allow site-specific coupling of immunogenic peptides are reported. Each of the modified proteins has a single free amino group; the other amino groups of lysine or the amino terminus

Actin dynamics studied by solid-state NMR spectroscopy.

L Phillips et al.

European biophysics journal : EBJ, 19(3), 147-155 (1991-01-01)

Solid-state nuclear magnetic resonance spectroscopy was used to study the motion of 2H and 19F probes attached to the skeletal muscle actin residues Cys-10, Lys-61 and Cys-374. The probe resonances were observed in dried and hydrated G-actin, F-actin and F-actin-myosin

Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry.

R L Beardsley et al.

Rapid communications in mass spectrometry : RCM, 14(23), 2147-2153 (2000-12-13)

Tryptic digests of three proteins are reacted with O-methylisourea in order to convert lysine residues to homoarginines. The resulting homoarginine-terminated peptides exhibit more intense MALDI mass spectral peaks than their lysine-terminated predecessors. This simple chemical reaction should therefore facilitate protein

Enrichment and analysis of peptide subsets using fluorous affinity tags and mass spectrometry.

Scott M Brittain et al.

Nature biotechnology, 23(4), 463-468 (2005-03-16)

Although mass spectrometry has become a powerful tool for the functional analysis of biological systems, complete proteome characterization cannot yet be achieved. Instead, the sheer complexity of living organisms demands fractionation of cellular extracts to enable more targeted analyses. Here

Kinetics of chemical modification of arginine and lysine residues in calf thymus histone H1.

K Mita et al.

Biopolymers, 20(6), 1103-1112 (1981-06-01)

Derivatization procedures to facilitate de novo sequencing of lysine-terminated tryptic peptides using postsource decay matrix-assisted laser desorption/ionization mass spectrometry.

T Keough et al.

Rapid communications in mass spectrometry : RCM, 14(24), 2348-2356 (2000-12-13)

Guanidination of the epsilon-amino group of lysine-terminated tryptic peptides can be accomplished selectively in one step with O-methylisourea hydrogen sulfate. This reaction converts lysine residues into more basic homoarginine residues. It also protects the epsilon-amino groups against unwanted reaction with

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