Peptides from peptic digest of bovine DIP-tripsin and determination of disulfide bonds

1968 ◽  
Vol 33 (2) ◽  
pp. 441-461 ◽  
Author(s):  
V. Holeyšovský ◽  
B. Mesrob ◽  
V. Tomášek ◽  
O. Mikeš ◽  
F. Šorm
Keyword(s):  
Disulfide Bonds

Rapid and Sensitive Determination of Protein Disulfide Bonds

Proteins ◽  
1987 ◽  
pp. 493-501 ◽  
Author(s):  
Hsieng S. Lu ◽  
Michael L. Klein ◽  
Richard R. Everett ◽  
Por-Hsiung Lai
Keyword(s):  
Disulfide Bonds ◽  
Sensitive Determination ◽  
Protein Disulfide Bonds ◽  
Protein Disulfide

scholarly journals THE IMPORTANCE OF THE FUNCTIONAL STATE OF THIOL-DISULFIDE UNIT OF THE ANTIOXIDANT SYSTEM IN THE ACUTE BACTERIAL DYSENTERY IN THE FORECAST OF THE COURSE AND THE SELECTION OF THE TREATMENT REGIMEN

2017 ◽  
Vol 22 (5) ◽  
pp. 258-263
Author(s):  
Zarema G. Tagirova
Keyword(s):  
Antimicrobial Peptides ◽  
Functional State ◽  
Antioxidant System ◽  
Disulfide Bonds ◽  
Severe Disease ◽  
Treatment Methods ◽  
Sh Groups ◽  
Group I ◽  
Antioxidant Agents

The goal was to optimize the treatment of shigellosis patients on the basis of an evaluation of the functional state of the thiol-disulfide unit of the antioxidant system (AOS) on a background of various treatment methods. Materials and methods. 400 patients with acute bacterial dysentery of varying severity of the course were observed; Shigella Flexner was isolated in 324(81%) cases, Shigella Sonne - in 76(19%) cases. The determination of sulfhydryl (SH-) groups and disulfide bonds (SS-) was carried out by the direct and reverse amperometric titration with the use of silver nitrate and unithiol in hemolysate. Three groups separated by random sampling were considered. In group I (122 patients), basic therapy was prescribed, including etiotropic and pathogenetic treatment. In group II (134 patients), pathogenetic treatment was prescribed in the combination with a complex of natural cytokines and antimicrobial peptides secreted by pig peripheral blood leukocytesa (»superlimph» preparation). In the third group (144 patients), the drug «superlimph» was prescribed along with etiotropic and pathogenetic treatment. Results. In acute bacterial dysentery disturbances of the redox balance were established to be correlated with the severity of the course in the form of a significant decrease in the level of SH-groups and the thiol-disulfide coefficient on the background of an increase in the level of SS-groups, which indicates to a decrease in the buffer capacity of the AOS. These data can serve as predictors of the nature of the course of dysentery. Comparative clinical evaluation of the effectiveness of various treatment methods revealed the most pronounced in severe disease advantages of complex therapy, including a combination of basic etiotropic, pathogenetic treatment with a complex of natural cytokines and antimicrobial peptides («superlimph»). Conclusion. The change in the ratio of oxidative processes to AOS occurs at any severity of dysentery, but in severe cases these changes acquire a qualitative character. In the survey standards for bacterial dysentery there is recommended to include the determination of indices of the thiol-disulfide unit, as an additional criterion for the severity of the course and the prognosis of the course of the disease. Exceeding the concentration of SS-groups of the concentration of SH-groups and the inversion of the thiol-disulfide coefficient as markers of the breakdown in AOS seem to be prognostically unfavorable factor. The severe course of acute bacterial dysentery is an indication for inclusion of antioxidant agents in the therapeutic complex. Based on the mechanism of revealed abnormalities in AOS, the use of a complex of natural cytokines and antimicrobial peptides («superlimph») can be considered as an immunocorrecting drug.

scholarly journals Determination of the Disulfide Bonds within a B Domain Variant Surface Glycoprotein fromTrypanosoma congolense

1998 ◽  
Vol 273 (49) ◽  
pp. 32582-32586 ◽  
Author(s):  
Holm Bußler ◽  
Monica Linder ◽  
Dietmar Linder ◽  
Erwin Reinwald
Keyword(s):  
Disulfide Bonds ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Domain Variant

scholarly journals Determination of disulfide bonds in 8.2 S globulin of cotton seeds

1971 ◽  
Vol 7 (6) ◽  
pp. 848-848
Author(s):  
Kh. Mirzarakhmatov ◽  
P. Kh. Yuldashev
Keyword(s):  
Disulfide Bonds ◽  
Cotton Seeds

scholarly journals Intermediate Detection in the Casiopeina–Cysteine Interaction Ending in the Disulfide Bond Formation and Copper Reduction

Molecules ◽  
2021 ◽  
Vol 26 (19) ◽  
pp. 5729
Author(s):  
Lillian G. Ramírez-Palma ◽  
Adrián Espinoza-Guillén ◽  
Fabiola Nieto-Camacho ◽  
Alexis E. López-Guerra ◽  
Virginia Gómez-Vidales ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Copper Complexes ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Cancer Therapies ◽  
Oxygen Species ◽  
Present Evidence ◽  
Endogenous Antioxidant ◽  
Tumoral Cells

A strategy to improve the cancer therapies involves agents that cause the depletion of the endogenous antioxidant glutathione (GSH), increasing its efflux out of cells and inducing apoptosis in tumoral cells due to the presence of reactive oxygen species. It has been shown that Casiopeina copper complexes caused a dramatic intracellular GSH drop, forming disulfide bonds and reducing CuII to CuI. Herein, through the determination of the [CuII]–SH bond before reduction, we present evidence of the adduct between cysteine and one Casiopeina as an intermediate in the cystine formation and as a model to understand the anticancer activity of copper complexes. Evidence of such an intermediate has never been presented before.

scholarly journals Characterisation of a Novel A-Superfamily Conotoxin

Biomedicines ◽  
2020 ◽  
Vol 8 (5) ◽  
pp. 128
Author(s):  
David T. Wilson ◽  
Paramjit S. Bansal ◽  
David A. Carter ◽  
Irina Vetter ◽  
Annette Nicke ◽  
...  
Keyword(s):  
Nicotinic Acetylcholine Receptor ◽  
Disulfide Bonds ◽  
Three Dimensional ◽  
Structural Type ◽  
Dimensional Structure ◽  
Na Channels ◽  
Nicotinic Acetylcholine ◽  
Therapeutic Leads ◽  
Helical Region

Conopeptides belonging to the A-superfamily from the venomous molluscs, Conus, are typically α-conotoxins. The α-conotoxins are of interest as therapeutic leads and pharmacological tools due to their selectivity and potency at nicotinic acetylcholine receptor (nAChR) subtypes. Structurally, the α-conotoxins have a consensus fold containing two conserved disulfide bonds that define the two-loop framework and brace a helical region. Here we report on a novel α-conotoxin Pl168, identified from the transcriptome of Conus planorbis, which has an unusual 4/8 loop framework. Unexpectedly, NMR determination of its three-dimensional structure reveals a new structural type of A-superfamily conotoxins with a different disulfide-stabilized fold, despite containing the conserved cysteine framework and disulfide connectivity of classical α-conotoxins. The peptide did not demonstrate activity on a range of nAChRs, or Ca2+ and Na+ channels suggesting that it might represent a new pharmacological class of conotoxins.

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