scholarly journals Immunoglobulin G and bovine serum albumin streaming dielectrophoresis in a microfluidic device

2011 ◽  
pp. n/a-n/a ◽  
Author(s):  
Asuka Nakano ◽  
Tzu-Chiao Chao ◽  
Fernanda Camacho-Alanis ◽  
Alexandra Ros
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Microfluidic Device ◽  
Immunoglobulin G ◽  
Bovine Serum

The Solubility of Insect Juvenile Hormone in Aqueous Solutions and Its Adsorption by Glassware and Plastics

1977 ◽  
Vol 32 (3-4) ◽  
pp. 158-160 ◽  
Author(s):  
Ch. Giese ◽  
K. D. Spindler ◽  
H. Emmerich
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Juvenile Hormone ◽  
Immunoglobulin G ◽  
Bovine Serum ◽  
Plastic Materials ◽  
Buffer Composition ◽  
Ph Buffer

Abstract The C18 juvenile hormone of insects can be dissolved in aqueous solutions up to a concentration of 2.5 - 3.0 × 10-5 M; changes in pH, buffer composition and ionic strength hardly affect this solu­bility. The hormone is salted out gradually by increasing ammonium sulphate concentrations. The juvenile hormone is bound to proteins such as bovine serum albumin or goat immunoglobulin G and can be kept in solution by these proteins up to 10-3 M. The hormone is strongly absorbed by many commonly used plastic materials but only to a lesser extent by glass and teflon.

Rapid detection of Cu2+ by a paper-based microfluidic device coated with bovine serum albumin (BSA)–Au nanoclusters

The Analyst ◽  
2015 ◽  
Vol 140 (22) ◽  
pp. 7823-7826 ◽  
Author(s):  
Xueen Fang ◽  
Qianqian Zhao ◽  
Hongmei Cao ◽  
Juan Liu ◽  
Ming Guan ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Microfluidic Device ◽  
Bovine Serum ◽  
Rapid Detection ◽  
Au Nanoclusters

In this work, bovine serum albumin (BSA)–Au nanoclusters were used to coat a paper-based microfluidic device.

scholarly journals Correction: Rapid detection of Cu2+ by a paper-based microfluidic device coated with bovine serum albumin (BSA)–Au nanoclusters

The Analyst ◽  
2015 ◽  
Vol 140 (24) ◽  
pp. 8217-8217
Author(s):  
Xueen Fang ◽  
Qianqian Zhao ◽  
Hongmei Cao ◽  
Juan Liu ◽  
Ming Guan ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Microfluidic Device ◽  
Bovine Serum ◽  
Rapid Detection ◽  
Au Nanoclusters

Correction for ‘Rapid detection of Cu2+ by a paper-based microfluidic device coated with bovine serum albumin (BSA)–Au nanoclusters’ by Xueen Fang, et al., Analyst, 2015, 140, 7823–7826.

Interaction between Gold Nanoparticles and Bovine Serum Albumin or Sheep Antirabbit Immunoglobulin G

2006 ◽  
Vol 24 (2) ◽  
pp. 253-256 ◽  
Author(s):  
Li-Mei Ao ◽  
Feng Gao ◽  
Bi-Feng Pan ◽  
Da-Xiang Cui ◽  
Hong-Chen Gu
Keyword(s):  
Gold Nanoparticles ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Immunoglobulin G ◽  
Bovine Serum

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

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