Complexation of Bovine Serum Albumin and Sugar Beet Pectin: Structural Transitions and Phase Diagram

Langmuir ◽  
2012 ◽  
Vol 28 (27) ◽  
pp. 10164-10176 ◽  
Author(s):  
Xiangyang Li ◽  
Yapeng Fang ◽  
Saphwan Al-Assaf ◽  
Glyn O. Phillips ◽  
Xiaolin Yao ◽  
...  
Keyword(s):  
Phase Diagram ◽  
Bovine Serum Albumin ◽  
Sugar Beet ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Structural Transitions

Photoacids as a new fluorescence tool for tracking structural transitions of proteins: following the concentration-induced transition of bovine serum albumin

2015 ◽  
Vol 17 (47) ◽  
pp. 32023-32032 ◽  
Author(s):  
Nadav Amdursky
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Structural Transition ◽  
Low Ph ◽  
Special Focus ◽  
Structural Transitions

The concentration-induced structural transition of BSA at low pH was studied with photoacids. A special focus is also given to the discussion about the validity of other techniques to observe this transition.

Genipin-crosslinked sugar beet pectin-bovine serum albumin nanoparticles as novel pickering stabilizer

2021 ◽  
Vol 112 ◽  
pp. 106306
Author(s):  
Jiawei Lin ◽  
Hecheng Meng ◽  
Shujuan Yu ◽  
Zhiming Wang ◽  
Chao Ai ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Sugar Beet ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Albumin Nanoparticles

Effects of bovine serum albumin on the ethanol precipitation of sugar beet pulp pectins

2020 ◽  
Vol 105 ◽  
pp. 105813
Author(s):  
Tao Zhang ◽  
Xiaoming Guo ◽  
Hecheng Meng ◽  
Xiangyi Tang ◽  
Chao Ai ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Sugar Beet ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sugar Beet Pulp ◽  
Ethanol Precipitation ◽  
Beet Pulp

Complexation of bovine serum albumin and sugar beet pectin: Stabilising oil-in-water emulsions

2012 ◽  
Vol 388 (1) ◽  
pp. 103-111 ◽  
Author(s):  
Xiangyang Li ◽  
Yapeng Fang ◽  
Saphwan Al-Assaf ◽  
Glyn O. Phillips ◽  
Fatang Jiang
Keyword(s):  
Bovine Serum Albumin ◽  
Sugar Beet ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Oil In Water

Thermo-reversibility, ergodicity and surface charge–temperature dependent phase diagram of anionic, cationic and neutral co-gels of gelatin–BSA complexes

RSC Advances ◽  
2016 ◽  
Vol 6 (46) ◽  
pp. 40123-40136 ◽  
Author(s):  
Jyotsana Pathak ◽  
Kamla Rawat ◽  
H. B. Bohidar
Keyword(s):  
Phase Diagram ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Mixing Ratio ◽  
Temperature Dependent ◽  
Gelation Behavior ◽  
Ph Range ◽  
Protein Bovine Serum Albumin ◽  
Charge Temperature

We have investigated the gelation behavior of polyampholyte gelatin B (GB) in the presence of colloidal plasma protein bovine serum albumin (BSA) as a function of mixing ratio (r = GB : BSA = 1.5–4), entire pH range, and temperature (20–45 °​C).

Robust W/O/W Emulsion Stabilized by Genipin-Cross-Linked Sugar Beet Pectin-Bovine Serum Albumin Nanoparticles: Co-encapsulation of Betanin and Curcumin

2021 ◽  
Vol 69 (4) ◽  
pp. 1318-1328
Author(s):  
Xiang-Yi Tang ◽  
Zhi-Ming Wang ◽  
He-Cheng Meng ◽  
Jia-Wei Lin ◽  
Xiao-Ming Guo ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Sugar Beet ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Albumin Nanoparticles

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

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