Studies on Coupling Pancreatic Ribonucléase and Bovine Serum Albumin through Disulfide Bonds / Letters to the Editors

1967 ◽  
Vol 8 (1) ◽  
pp. 73-80
Author(s):  
D. Frommel ◽  
H.C. Isliker ◽  
J. King ◽  
N. Dioguardi
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Pancreatic Ribonuclease

Bis(triethylphosphine)gold(I) chloride: ionization in aqueous solution, reduction in vitro of the external and internal disulfide bonds of bovine serum albumin and antiarthritic activity

1989 ◽  
Vol 28 (7) ◽  
pp. 1321-1326 ◽  
Author(s):  
Anvarhusein A. Isab ◽  
Anne L. Hormann ◽  
David T. Hill ◽  
Don E. Griswold ◽  
Michael J. DiMartino ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Disulfide Bonds

scholarly journals An All-Atomistic Molecular Dynamics Study to Determine the Structural Importance of Disulfide Bonds in Immunoglobulin G and Bovine Serum Albumin

2018 ◽  
Vol 15 (1) ◽  
Author(s):  
Akshay Mathavan ◽  
Akash Mathavan ◽  
Michael Fortunato ◽  
Coray Colina
Keyword(s):  
Molecular Dynamics ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunoglobulin G ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Structural Changes ◽  
Conformational Stability ◽  
The Stability

A fully-atomistic molecular dynamics study was performed to determine the importance of disulfide bonds on the stability of immunoglobulin G (IgG) and bovine serum albumin (BSA).The transferability of a previous prescreening methodology to assess contributions from individual disulfide bonds on conformational stability was tested on both proteins. In IgG, it was apparent that inter-chain and intra-chain disulfide bonds play different roles in maintaining structure, evidenced by clear separation of inter-chain cysteine residues upon cleavage of disulfide bonds. In BSA, a set of double disulfide bonds required both to be broken in order to observe significant structural changes, equivalently seen in a previous study of human serum albumin (HSA), a structurally similar protein. Structural analysis of IgG showed deviations in distances between domains, while analysis of BSA suggested more local structural changes. This work helps confirm the efficacy and reproducibility of the prescreening methodology on both a novel, larger protein such as IgG and a more homologous (to HSA), globular protein such as BSA. The results provide insight into the role of specific disulfide bonds in the stability of IgG and BSA. KEYWORDS: Molecular Dynamics; Atomistic Simulations; Immunoglobulin G; Bovine Serum Albumin; Disulfide Bonds

scholarly journals Anti-aggregation effect of Ascorbic Acid and Quercetin on aggregated Bovine Serum Albumin Induced by Dithiothreitol: Comparison of Turbidity and Soluble Protein Fraction Methods

2020 ◽  
Vol 23 (4) ◽  
pp. 129-134
Author(s):  
Amat Rifai ◽  
Mukhammad Asy'ari ◽  
Agustina L. N. Aminin
Keyword(s):  
Ascorbic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Aggregation ◽  
Soluble Protein ◽  
Bovine Serum ◽  
Disulfide Bonds ◽  
Protein Profile ◽  
Turbidity Method ◽  
Aggregation Activity

Studies on the anti-aggregation of dithiothreitol (DTT) induced - protein is generally determined by the fraction soluble (non-aggregated) protein. While the turbidity method is commonly used in studies of anti-aggregation, in which protein is induced by heat, in this study, both methods are compared in observing the anti-aggregation activity of ascorbic acid and quercetin toward bovine serum albumin induced by DTT. The DTT is a reducing agent for protein disulfide bonds and capable of inducing protein aggregation at physiological pH and temperature. The work was performed by the formation of Bovine Serum Albumin (BSA) aggregates induced by DTT under physiological conditions, which are pH 7.4 and 37°C. The aggregated protein profile was observed using the turbidity method at the end of incubation and measuring the difference of concentration between the fraction of soluble protein before and after incubation. The measurement was carried out using a spectrophotometer UV-Vis. The results indicate that both methods show similar inhibition profiles. The potential inhibition of ascorbic acid (AA) toward BSA protein aggregation induced by DTT increased along with incubation time. While quercetin shows the highest inhibition at 12 hours but decreased at 18 hours, this study reveals that both methods can observe the anti-aggregation activity of ascorbic acid and quercetin.

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