Utilization of L-Methionine Sulfoxide, L-Methionine Sulfone and Cysteic Acid by the Weanling Rat

1976 ◽  
Vol 106 (8) ◽  
pp. 1108-1114 ◽  
Author(s):  
G. Harvey Anderson ◽  
David V. M. Ashley ◽  
John D. Jones
Keyword(s):  
Methionine Sulfoxide ◽  
Cysteic Acid ◽  
Methionine Sulfone

scholarly journals Determination of Sulfur Amino Acids in Foods as Related to Bioavailability

2008 ◽  
Vol 91 (4) ◽  
pp. 907-913 ◽  
Author(s):  
Shane M Rutherfurd ◽  
Paul J Moughan
Keyword(s):  
Methionine Sulfoxide ◽  
Performic Acid ◽  
Cysteic Acid ◽  
Acid Oxidation ◽  
Separate Determination ◽  
Sulfur Amino Acids ◽  
Methionine Sulfone ◽  
Quantitative Impact ◽  
Selection Of

Abstract During the processing of feedstuffs and foods, methionine can be oxidized to methionine sulfoxide and methionine sulfone, and cysteine can be oxidized to cysteic acid. Methionine sulfone and cysteic acid are nutritionally unavailable, but methionine sulfoxide can be utilized, at least to some degree. The degree of utilization depends on the levels of methionine, cysteine, and methionine sulfoxide in the diet, but there is no consensus in the literature on the quantitative impact of these dietary constituents on methionine sulfoxide utilization. Methionine and cysteine are most often determined after quantitative oxidation to methionine sulfone and cysteic acid, respectively, using performic acid oxidation prior to hydrolysis. However, this method may overestimate the methionine content of processed foods, as it will include any methionine sulfoxide and methionine sulfone present. A selection of analytical methods has been developed to allow the separate determination of the 3 oxidized forms of methionine, the merits of which are discussed in this review. An additional consideration for determining methionine and cysteine bioavailability is that not all dietary methionine and cysteine is digested and absorbed from the small intestine. Selected methods designed to determine the extent of digestion and absorption are discussed. Finally, a concept for a new assay for determining methionine bioavailability, which includes determining the digestibility of methionine and methionine sulfoxide as well as the utilization of methionine sulfoxide, is presented.

EFFECT OF SULFUR COMPOUNDS ON APPRESSORIUM FORMATION BY COLLETOTRICHUM GRAMINICOLA

1971 ◽  
Vol 51 (1) ◽  
pp. 49-51 ◽  
Author(s):  
H. J. NETOLITZKY ◽  
W. P. SKOROPAD
Keyword(s):  
Reduced Glutathione ◽  
Methionine Sulfoxide ◽  
Sulfhydryl Groups ◽  
Cysteic Acid ◽  
Colletotrichum Graminicola ◽  
Appressorium Formation ◽  
Cysteine Sulfinic Acid ◽  
Homocysteic Acid ◽  
Methionine Sulfone

Compounds containing sulfhydryl groups inhibited appressorium formation by Colletotrichum graminicola (Ces.) Wils. Appressoria were not formed in 0.03 and 0.06 M solutions of cysteine, homocysteine, thiohistidine and reduced glutathione. They were formed abundantly within 24 hr in 0.006, 0.03 and 0.06 M solutions of cysteine sulfinic acid, cysteic acid, homocysteic acid, S-methyl cysteine, methionine, methionine sulfone, methionine sulfoxide, and oxidized glutathione. The role of sulfhydryl groups in the inhibition of appressorium formation is discussed.

scholarly journals Structural Basis of Peroxide-mediated Changes in Human Hemoglobin

2006 ◽  
Vol 282 (7) ◽  
pp. 4894-4907 ◽  
Author(s):  
Yiping Jia ◽  
Paul W. Buehler ◽  
Robert A. Boykins ◽  
Richard M. Venable ◽  
Abdu I. Alayash
Keyword(s):  
Structural Changes ◽  
Blood Substitute ◽  
Methionine Sulfoxide ◽  
Reversed Phase ◽  
Cysteic Acid ◽  
Structural Basis ◽  
Human Hemoglobin ◽  
Peptide Fragments ◽  
Oxidative Pathway ◽  
First Time

Hydrogen peroxide (H2O2) triggers a redox cycle between ferric and ferryl hemoglobin (Hb) leading to the formation of a transient protein radical and a covalent hemeprotein cross-link. Addition of H2O2 to highly purified human hemoglobin (HbA0) induced structural changes that primarily resided within β subunits followed by the internalization of the heme moiety within α subunits. These modifications were observed when an equal molar concentration of H2O2 was added to HbA0 yet became more abundant with greater concentrations of H2O2. Mass spectrometric and amino acid analysis revealed for the first time that βCys-93 and βCys-112 were oxidized extensively and irreversibly to cysteic acid when HbA0 was treated with H2O2. Oxidation of further amino acids in HbA0 exclusive to the β-globin chain included modification of βTrp-15 to oxyindolyl and kynureninyl products as well as βMet-55 to methionine sulfoxide. These findings may therefore explain the premature collapse of the β subunits as a result of the H2O2 attack. Analysis of a tryptic digest of the main reversed phase-high pressure liquid chromatography fraction revealed two α-peptide fragments (α128 - α139) and a heme moiety with the loss of iron, cross-linked between αSer-138 and the porphyrin ring. The novel oxidative pathway of HbA0 modification detailed here may explain the diverse oxidative, toxic, and potentially immunogenic effects associated with the release of hemoglobin from red blood cells during hemolytic diseases and/or when cell-free Hb is used as a blood substitute.

Oxidation and Hydrolysis Determination of Sulfur Amino Acids in Food and Feed Ingredients: Collaborative Study

1985 ◽  
Vol 68 (5) ◽  
pp. 826-829 ◽  
Author(s):  
John L Macdonald ◽  
Mark W Krueger ◽  
John H Keller
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Performic Acid ◽  
Cysteic Acid ◽  
Feed Ingredients ◽  
Methionine Sulfone ◽  
Coefficients Of Variation ◽  
Food And Feed ◽  
The Mean

Abstract Samples of 6 food and feed ingredients and a purified protein, plactoglobulin, were analyzed by 7 laboratories to determine the concentrations of cysteine as cysteic acid and methionine as methionine sulfone. Samples were oxidized by reaction with performic acid before hydrolysis with 6N HC1. The free amino acids were then separated and measured by ion-exchange chromatography on dedicated amino acid analyzers. Each laboratory was provided with a detailed method as well as sealed vials containing solutions of standards. For the determination of cysteine as cysteic acid, the coefficients of variation between laboratories for duplicate samples ranged from 7.13 to 10.8% for the 6 ingredients. For the determination of methionine as methionine sulfone, the coefficients of variation between laboratories for duplicate samples ranged from 1.18 to 12.8% for the 6 ingredients. Cysteine and methionine recoveries were determined by analysis of β-Iactoglobulin and were based on expected levels of each amino acid from amino acid sequence data. The mean recovery of cysteine was 95% with a range of 91-101%. The mean recovery of methionine was 101% with a range of 98-106%. This method has been adopted official first action.

Ochratoxin production by Aspergillus ochraceus as affected by methionine and structurally related compounds

1983 ◽  
Vol 29 (5) ◽  
pp. 536-540 ◽  
Author(s):  
N. Lisker ◽  
N. Paster ◽  
I. Chet
Keyword(s):  
Radial Growth ◽  
Sole Carbon Source ◽  
Synthetic Medium ◽  
Methionine Sulfoxide ◽  
Dry Weight ◽  
Aspergillus Ochraceus ◽  
Inhibitory Effects ◽  
Methionine Sulfone ◽  
Initial Ph ◽  
Related Compounds

When 10−2 M of L- or D-methionine was added to a synthetic medium containing xylose as the sole carbon source, ochratoxin production by Aspergillus ochraceus was strongly inhibited. At that concentration methionine derivatives, e.g., α-methyl-DL-methionine, DL-methionine sulfoxide, and L-methionine sulfone, did not inhibit ochratoxin production, whereas DL-methionine S-methyl sulfonium chloride (MMSC) inhibited ochratoxin production to a large extent. L-Methionine, as well as MMSC, also completely inhibited sclerotia formation, while D-methionine and DL-methionine sulfoxide caused only a partial inhibition. At lower concentrations (10−3 and 10−4 M), none of the compounds exhibited inhibitory effects. In cases where strong ochratoxin inhibition was detected, fungal radial growth or mycelial dry weight was inhibited by only 10–25%, while the initial pH of the medium dropped from ~6.5 to ~4.4–5.0. Adjustment of the initial pH of media supplemented with 10−2 ML-methionine, D-methionine, or MMSC to a pH of ~7.8 did not change the inhibitory effects on ochratoxin production in media containing L-methionine. On the other hand, sclerotia formation was restored in all three treatments.

scholarly journals Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase

Molecules ◽  
2021 ◽  
Vol 26 (17) ◽  
pp. 5344
Author(s):  
Darren Leahy ◽  
Cameron Grant ◽  
Alex Jackson ◽  
Alex Duff ◽  
Nicholas Tardiota ◽  
...  
Keyword(s):  
Tissue Damage ◽  
Neutrophil Elastase ◽  
Human Neutrophil ◽  
Critical Role ◽  
Methionine Sulfoxide ◽  
Chronic Obstructive ◽  
Human Neutrophil Elastase ◽  
Obstructive Pulmonary Disease ◽  
Methionine Residue ◽  
Methionine Sulfone

Human neutrophil elastase (HNE) is a uniquely destructive serine protease with the ability to unleash a wave of proteolytic activity by destroying the inhibitors of other proteases. Although this phenomenon forms an important part of the innate immune response to invading pathogens, it is responsible for the collateral host tissue damage observed in chronic conditions such as chronic obstructive pulmonary disease (COPD), and in more acute disorders such as the lung injuries associated with COVID-19 infection. Previously, a combinatorially selected activity-based probe revealed an unexpected substrate preference for oxidised methionine, which suggests a link to oxidative pathogen clearance by neutrophils. Here we use oxidised model substrates and inhibitors to confirm this observation and to show that neutrophil elastase is specifically selective for the di-oxygenated methionine sulfone rather than the mono-oxygenated methionine sulfoxide. We also posit a critical role for ordered solvent in the mechanism of HNE discrimination between the two oxidised forms methionine residue. Preference for the sulfone form of oxidised methionine is especially significant. While both host and pathogens have the ability to reduce methionine sulfoxide back to methionine, a biological pathway to reduce methionine sulfone is not known. Taken together, these data suggest that the oxidative activity of neutrophils may create rapidly cleaved elastase “super substrates” that directly damage tissue, while initiating a cycle of neutrophil oxidation that increases elastase tissue damage and further neutrophil recruitment.

scholarly journals DNA Synthesis in Relation to Hyphal Branching and Wall Composition in Allomyces macrogynus

1985 ◽  
Vol 38 (1) ◽  
pp. 67 ◽  
Author(s):  
Jean Youatt
Keyword(s):  
Dna Synthesis ◽  
Sodium Sulfide ◽  
Methionine Sulfoxide ◽  
Cylindrical Shape ◽  
Sulfur Amino Acids ◽  
Hyphal Branching ◽  
The Third ◽  
Methionine Sulfone ◽  
Allomyces Macrogynus ◽  
Hyphal Tip

In A. macrogynus the first replication of DNA occurred after germination, at the time of the first branching of rhizoids. Before the second replication galactan in the wall exceeded the glucan content and was not firmly attached. After the second DNA replication hyphallengthening commenced with an increase in the content of glucan but the walls lacked rigidity. At the time of the third replication walls underwent a change which commenced at the hyphal tip and worked back to the rhizoids, converting the hyphae to a rigid, cylindrical shape. Branching commenced after the fourth replication of DNA. Multiple branching occurred when mature plants were transferred to glucose-histidine-methionine solution without further DNA synthesis. Hyphal branching was used to show that A. macrogynus was able to use methionine, methionine sulfoxide, methionine sulfone, sodium sulfide, cysteine, cystathionine and homocysteine but not cystine. Thioacetamide supported growth through many subcultures showing that A. macrogynus can synthesize its sulfur amino acids.

The effects of selenium on the metabolism of methionine in sheep

1976 ◽  
Vol 54 (3) ◽  
pp. 336-346 ◽  
Author(s):  
M. Hidiroglou ◽  
C. G. Zarkadas
Keyword(s):  
Plasma Proteins ◽  
Selenium Supplementation ◽  
Cysteic Acid ◽  
Methionine Metabolism ◽  
Selenium Status ◽  
Bacterial Protein ◽  
Bacterial Proteins ◽  
Methionine Sulfone ◽  
Rumen Microflora ◽  
Low Levels

Two groups of sheep fed a diet of hay known to produce nutritional muscular dystrophy, one group of which received selenium supplementation, were used to study the effects of selenium on the metabolism of administered L-[35S](methionine by rumen microflora. Rumen bacterial proteins of the Se supplemented sheep contained significantly higher levels of radiosulfur than the bacterial protein of the non-supplemented sheep. Of the L-[35S]methionine present in the rumen liquor samples from Se-supplemented sheep 2 h after administration, 13.3% of the amino acid, which was measured as methionine sulfone, was found in the microbial proteins. A large proportion of the administered labeled methionine was resynthesized as cyst(e)ine which may account in part for that determined as cysteic acid in rumen bacterial and plasma proteins. The observed low levels of radiosulfur found in rumen microflora from selenium deficient wethers, indicates that the presence of selenium profoundly affects the rate of methionine metabolism and the distribution of methionine in rumen bacterial and protozoal proteins.In another experiment, the effect of selenium on the metabolism of L-[Me-3H]methionine was studied. The selenium status of the sheep had no significant effect (P > 0.05) on the distribution of 35S radioactivity in the blood plasma and tissues.

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