Conformational Change of Bovine Serum Albumin Molecules at Neutral pH in Ultra-Diluted Aqueous Solutions

2014 ◽  
Vol 118 (42) ◽  
pp. 12207-12214 ◽  
Author(s):  
Shulian He ◽  
Mei Huang ◽  
Wei Ye ◽  
Dechao Chen ◽  
Shuai He ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Conformational Change ◽  
Bovine Serum ◽  
Neutral Ph

scholarly journals pK change of imidazole groups in bovine serum albumin due to the conformational change at neutral pH

Biochemistry ◽  
1971 ◽  
Vol 10 (17) ◽  
pp. 3217-3221 ◽  
Author(s):  
S. H. De Bruin ◽  
B. J. M. Harmsen ◽  
L. H. M. Janssen ◽  
J. F. Rodrigues de Miranda ◽  
G. A. J. Van Os
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Change ◽  
Bovine Serum ◽  
Neutral Ph

Development and creation of zeta potential reference material of the particles in a liquid medium

2021 ◽  
pp. 58-62
Author(s):  
Dmitrii I. Belenkii ◽  
Dmitry V. Averkin ◽  
Dmitry V. Vishnevetskii ◽  
Svetlana D. Khizhnyak ◽  
Pavel M. Pakhomov
Keyword(s):  
Bovine Serum Albumin ◽  
Zeta Potential ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Bovine Serum ◽  
Polystyrene Latex ◽  
Powder Materials ◽  
Silver Acetate ◽  
Supramolecular Systems ◽  
Standard Samples

A comprehensive study to develop and create standard samples of the zeta potential unit of particles in a liquid in accordance with the requirements of GOST ISO 13099-2-2016 in the range of measured values from minus 150 mV to plus 150 mV was carried out. The existing standard samples of zeta potential in Russia and the world have been investigated; the analysis of the applicability of the starting materials and components for the creation of new standard samples has done. Samples based on modified polystyrene latex microspheres, bovine serum albumin and supramolecular systems based on aqueous solutions of L-cysteine, N-acetylcysteine, and silver acetate were considered as promising standard samples of the zeta potential of particles. All studies were carried out on equipment from the State Primary Standard of Dispersed Parameters of Aerosols, Suspensions and Powder Materials GET 163-2020 using the method of electrophoretic light scattering and measuring the pH value. It was found that polystyrene latex microspheres do not correspond to the requirements of the work in terms of developing a set of standard samples. Samples based on suspensions of bovine serum albumin do not correspond to the requirements of GOST ISO 13099-2-2016. Supramolecular systems based on aqueous solutions of L-cysteine, N-acetylcysteine, and silver acetate were proposed as standard samples. Such systems are characterized by the ability to modify the initial potential-determining layer of particles without changing their aggregate stability. Studies of the long-term stability of the developed standard samples of the zeta-potential unit of particles in a liquid have been carried out.

Constants of the Formation of Complexes with Nanomarkers of the Fluorescein Family and Bovine Serum Albumin in Aqueous Solutions

2020 ◽  
Vol 94 (1) ◽  
pp. 152-157
Author(s):  
I. M. Vlasova ◽  
A. A. Vlasov ◽  
A. A. Kuleshova ◽  
Yu. A. Gordeeva ◽  
A. M. Saletskii
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Bovine Serum ◽  
Formation Of Complexes

A direct comparison of the interaction of bovine serum albumin and gelatin with sodium deoxycholate in aqueous solutions

2015 ◽  
Vol 207 ◽  
pp. 164-170 ◽  
Author(s):  
Huaying Ren ◽  
Xia Xin ◽  
Lin Wang ◽  
Huanfeng Ju ◽  
A'Dila Zhamanding ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Bovine Serum ◽  
Sodium Deoxycholate

Pressure Jump Studies of Proteins. I. Isomerization of Bovine Serum Albumin at Neutral pH

1971 ◽  
Vol 49 (12) ◽  
pp. 1267-1275 ◽  
Author(s):  
D. E. Goldsack ◽  
P. M. Waern
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Conformational Change ◽  
Bovine Serum ◽  
Ph Dependence ◽  
Kinetic Studies ◽  
Relaxation Effect ◽  
Pressure Jump ◽  
Relaxation Effects ◽  
Ph Range

Pressure jump kinetic studies of the conformational change occurring in bovine serum albumin in neutral solutions have been carried out over the pH range 6.5–9.5. Two distinct relaxation effects are observed at each pH. The faster relaxation is attributed to binding of the dye to the protein, and the slower relaxation is related to the conformational change occurring in the protein. This slower relaxation effect is pH dependent with a maximum value near pH 8. Detailed analysis of these data leads to a mechanism for the conformational change which indicates that the one form of the protein has an ionizable group with a pK of 8.7 which changes to a pK of 6.7 when the protein undergoes the conformational change. A simple iterative procedure is given for analyzing the pH dependence of a relaxation time constant for a cyclic mechanism involving only one ionizing group controlling the conformational change.

Sign in / Sign up

Export Citation Format

Share Document