The use of 3-bromopropionic acid for the determination of protein thiol groups

1973 ◽  
Vol 133 (4) ◽  
pp. 609.b1-609.b1
Keyword(s):  
Thiol Groups ◽  
Protein Thiol

scholarly journals The use of 3-bromopropionic acid for the determination of protein thiol groups

1973 ◽  
Vol 131 (4) ◽  
pp. 637-642 ◽  
Author(s):  
A. F. Bradbury ◽  
D. G. Smyth
Keyword(s):  
Carboxylic Acid ◽  
Intramolecular Cyclization ◽  
Iodoacetic Acid ◽  
Cyclization Reaction ◽  
Thiol Groups ◽  
Protein Thiol

S-Carboxymethylcysteine, formed by the reaction of iodoacetic acid with cysteine, was found to undergo intramolecular cyclization to yield 3-oxo-(2H,3H,5H,6H-1,4-thiazine)-5-carboxylic acid. The cyclization was studied under various conditions and the product was isolated and characterized. S-Carboxyethylcysteine, formed by the reaction of 3-bromopropionic acid with cysteine, did not undergo the cyclization reaction. The use of 3-bromopropionic acid was examined as an alternative to iodoacetic acid for the protection and determination of protein thiol groups.

Effect of Vernonia cognata on oxidative damage induced by ethanol in rats

2010 ◽  
Vol 30 (7) ◽  
pp. 675-684 ◽  
Author(s):  
CS Mota ◽  
RB Freitas ◽  
ML Athayde ◽  
AA Boligon ◽  
PR Augusti ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
High Performance ◽  
Tissue Injury ◽  
Antioxidant Effect ◽  
Gastric Tissue ◽  
Thiol Groups ◽  
Protein Thiol ◽  
Stress Markers ◽  
Hydroethanolic Extract ◽  
And Oxidative Stress

Free radicals production and oxidative stress play a central role in injuries caused by ethanol (EtOH) on gastric mucosal. Thus, strategies to counteract EtOH toxicity are highly desirable. This study was aimed at evaluating whether Vernonia cognata extract would reduce EtOH effects in rats. Rats received Vernonia cognata extract (0, 1 and 2 g/kg bw, by gavage) 1 hour after EtOH had been administered (0 or 70%, 0.5 mL/100 g bw, by gavage) and were killed 1 hour after Vernonia cognata extract administration. The stomach was removed for macroscopic and histopathological evaluation, as well as, oxidative stress markers such as lipoperoxidation (LPO) and non-protein thiol groups (NPSH) levels and catalase (CAT) activity. EtOH acute exposure increased LPO and decreased NPSH levels and CAT activity along with macroscopic and microscopic lesions in gastric tissue, confirming the involvement of oxidative stress in EtOH toxicity. Vernonia cognata extract attenuated oxidative and histopathological features induced by EtOH at all evaluated doses. Moreover, both studied doses of Vernonia cognata extract caused an increase in NPSH levels per se. However, only the dose of 2 g/kg reverted all macroscopic changes caused by EtOH toxicity. The protective effect of the extract could be attributed to antioxidant molecules present in the extract, such as flavonoids and phenolic acids, which were quantified by high performance liquid chromatography (HPLC). Thus, an antioxidant effect of the extract leads to a protection on gastric tissue. Our results indicate that Vernonia cognata hydroethanolic extract could have a beneficial role against EtOH toxicity by preventing oxidative stress and gastric tissue injury.

Determination of thiol groups with o-diacetoxy-iodobenzoate

Talanta ◽  
1977 ◽  
Vol 24 (8) ◽  
pp. 517-518 ◽  
Author(s):  
A Srivastava
Keyword(s):  
Thiol Groups

scholarly journals Markers of oxidative and antioxidative activity in female dogs with mammary gland tumour with and without additional vitamin E supplementation

2012 ◽  
Vol 81 (3) ◽  
pp. 275-280 ◽  
Author(s):  
Renata Stavinohová ◽  
Jana Lorenzová ◽  
Ivana Papežíková ◽  
Ivana Borkovcová ◽  
Jakub Pfeifr ◽  
...  
Keyword(s):  
Mammary Gland ◽  
Vitamin E ◽  
Antioxidative Activity ◽  
Thiobarbituric Acid ◽  
Thiol Groups ◽  
Thiobarbituric Acid Reactive Substances ◽  
Protein Thiol ◽  
Antioxidative Status ◽  
Group 2 ◽  
Gland Tumour

The present study determined markers of oxidative and antioxidative activity in dog females affected with mammary gland tumour compared to healthy ones. The effect of additional vitamin E supplementation on oxidative and antioxidative status was evaluated as well. The study included 29 female dogs divided into 4 groups (groups 1 and 2 included females with a mammary gland tumour; groups 3 and 4 included healthy female dogs). Additional vitamin supplement containing α-tocopherol was given to the females of groups 1 and 4. Dogs from groups 1 and 2 were anaesthetized before surgery (ovariohysterectomy and mastectomy); anaesthesia was used also in group 3, but without performeing surgery. The content of vitamin E (free α-tocopherol), marker of antioxidative status, was measured in blood serum by liquid chromatography. The concentration of thiobarbituric acid reactive substances, marker of oxidative status, in serum and concentrations of protein and non-protein thiol groups, markers of oxidative and antioxidative status, in blood serum and in red blood cells were measured colorimetrically. In females with a mammary gland tumour from group 2, concentration of thiobarbituric acid reactive substances was significantly higher than 14 days after surgery and compared to healthy ones as well. In females with a mammary gland tumour from group 2, concentration of protein thiol groups in serum was significantly lower and concentration of non-protein thiol groups in serum was significantly higher than in healthy controls. The values of protein thiols in erythrocytes in females with mammary gland tumour from group 1 were significantly higher before supplementation with vitamin E. The present study revealed that females with a mammary gland tumour were more burdened with oxidative stress compared to healthy dogs. The removal of the mammary gland tumour led to improvement of oxidative and antioxidative status. This is the first report focusing on the effect of additional α-tocopherol supplementation on reducing oxidative stress by increasing antioxidative activity in females affected with mammary gland tumour; however, we did not prove it.

scholarly journals Determination of Protein Thiol Reduction Potential by Isotope Labeling and Intact Mass Measurement

2016 ◽  
Vol 88 (5) ◽  
pp. 2727-2733 ◽  
Author(s):  
Sophie E. Thurlow ◽  
David P. Kilgour ◽  
Dominic J. Campopiano ◽  
C. Logan Mackay ◽  
Pat R. R. Langridge-Smith ◽  
...  
Keyword(s):  
Reduction Potential ◽  
Isotope Labeling ◽  
Mass Measurement ◽  
Protein Thiol ◽  
Intact Mass

scholarly journals The effect of tropomyosin on the adenosine triphosphatase activity of desensitized actomyosin

1967 ◽  
Vol 105 (3) ◽  
pp. 1235-1243 ◽  
Author(s):  
M. C. Schaub ◽  
S V Perry ◽  
D. J. Hartshorne
Keyword(s):  
Acetic Acid ◽  
Inhibitory Activity ◽  
Adenosine Triphosphatase ◽  
Inhibitory Effect ◽  
Tryptic Digestion ◽  
Prolonged Treatment ◽  
Thiol Groups ◽  
Protein Thiol ◽  
Adenosine Triphosphatase Activity ◽  
Inhibitory Activities

1. Tropomyosin preparations of the Bailey type, and those prepared in the presence of dithiothreitol to prevent oxidation of protein thiol groups, inhibit the Ca2+-activated adenosine triphosphatase (ATPase) of desensitized actomyosin by up to 60%. 2. The inhibitory activity of myofibrillar extracts and tropomyosin survives various agents known to denature proteins but to the action of which tropomyosin is unusually stable, namely heating at 100° and mild tryptic digestion. It is destroyed by prolonged treatment with trypsin. 3. The ethylenedioxybis-(ethyleneamino)tetra-acetic acid (EGTA)-sensitizing factor present in extracts of natural actomyosin and myofibrils could be selectively destroyed, leaving unchanged the inhibitory effect on the Ca2+-activated ATPase. There was no correlation between the EGTA-sensitizing and the Ca2+-activated inhibitory activities of tropomyosin prepared under different conditions. 4. Optimum inhibition was achieved when tropomyosin and the myosin of desensitized actomyosin were present in approximately equimolar proportions. Tropomyosin had no effect on the Ca2+-activated ATPase of myosin measured under similar conditions. 5. Evidence is presented showing that the tropomyosin binds to desensitized actomyosin under the conditions in which the ATPase is inhibited.

THE ROLE OF THIOL GROUPS IN THE DEVELOPMENT OF RADIATION DAMAGE IN THYMOCYTES AND EHRLICH ASCITES CARCINOMA CELLS

1964 ◽  
Vol 42 (12) ◽  
pp. 1717-1727 ◽  
Author(s):  
J. F. Scaife
Keyword(s):  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Irradiation Damage ◽  
Thiol Groups ◽  
Protein Thiol ◽  
Ehrlich Ascites ◽  
X Irradiation ◽  
The Difference

The effect of 800–1000 rads of X-irradiation on the thiol content of thymocytes and Ehrlich ascites carcinoma cells has been compared. Four hours after irradiation there was a decrease in the non-protein thiol (NP.SH) content of thymus and thymocytes but no change in ascites cells. In both cells the main NP.SH compound was glutathione. There was no significant effect of irradiation on the protein thiol (P.SH) content of thymus or ascites cells, but there was a slight decrease in P.SH in thymocytes after 4 hours incubation. Isolated thymus nuclei showed an immediate small decrease in P.SH content following 800 rads in vitro. Nuclei isolated from rat thymus 1 hour after 1000 rads in vivo showed an increase in the SH content of the globulin fraction and a decrease in the SH content of the nucleohistones. The total SH content of thymocytes and ascites cells was reduced by slow diffusion of H2O2into the cell suspension, but no effect of prior irradiation on this decrease of SH was found. Inhibition of catalase in vivo and in vitro did not produce any of the morphological signs of irradiation damage in thymocytes. There was no effect of irradiation on the copper content of thymus, thymocytes, or ascites cells. The ratio of NP.SH/P.SH is higher in thymocytes than in ascites cells, but, allowing for the difference in cell size, the overall total thiol concentration was the same. Anoxia produced only a small increase in NP.SH content in both cells and a small and doubtful increase in P.SH. It is concluded that, if thiol groups are involved in cell sensitivity to radiation, only a small fraction of the total SH groups are involved at critical sites.

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