Identification of competitive inhibitors for bovine serum albumin from dynamic combinatorial libraries containing a bienzyme system

RSC Advances ◽  
2015 ◽  
Vol 5 (30) ◽  
pp. 23224-23228 ◽  
Author(s):  
Wei He ◽  
Zheng Fang ◽  
Zhao Yang ◽  
Dong Ji ◽  
Ketao Chen ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Size Exclusion Chromatography ◽  
Bovine Serum ◽  
Combinatorial Libraries ◽  
Size Exclusion ◽  
System P ◽  
Competitive Inhibitors ◽  
Exclusion Chromatography

Three dynamic combinatorial libraries (DCLs) have been generated by using esterification, combined with a protocol based on size-exclusion chromatography (SEC) and HRMS.

scholarly journals Correction: Identification of competitive inhibitors for bovine serum albumin from dynamic combinatorial libraries containing a bienzyme system

RSC Advances ◽  
2015 ◽  
Vol 5 (67) ◽  
pp. 54563-54563
Author(s):  
Wei He ◽  
Zheng Fang ◽  
Zhao Yang ◽  
Dong Ji ◽  
Ketao Chen ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Combinatorial Libraries ◽  
System P ◽  
Competitive Inhibitors

Correction for ‘Identification of competitive inhibitors for bovine serum albumin from dynamic combinatorial libraries containing a bienzyme system’ by Wei He et al., RSC Adv., 2015, 5, 23224–23228.

Ultrasensitive detection of nonlabelled bovine serum albumin using photothermal optical phase shift detection with UV excitation

The Analyst ◽  
2020 ◽  
Vol 145 (7) ◽  
pp. 2580-2585 ◽  
Author(s):  
Hisashi Shimizu ◽  
Shigenori Takeda ◽  
Kazuma Mawatari ◽  
Takehiko Kitamori
Keyword(s):  
Phase Shift ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Detection System ◽  
Ultrasensitive Detection ◽  
Optical Phase ◽  
System P ◽  
Shift Detection ◽  
Uv Excitation

Ultrasensitive detection of nonlabelled bovine serum albumin is performed in micro/nanofluidic chips using a photothermal optical phase shift (POPS) detection system.

Bovine serum albumin and myoglobin separation by size exclusion SMB

2020 ◽  
Vol 1628 ◽  
pp. 461431
Author(s):  
Albertina G. Rios ◽  
Ana M. Ribeiro ◽  
Alírio E. Rodrigues ◽  
Alexandre F.P. Ferreira
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Size Exclusion

Analysis of cyclic polymer purity by size exclusion chromatography: a model system

2020 ◽  
Vol 11 (46) ◽  
pp. 7354-7361
Author(s):  
Yanlin Shi ◽  
Sung-Po R. Chen ◽  
Zhongfan Jia ◽  
Michael J. Monteiro
Keyword(s):  
Physical Properties ◽  
Size Exclusion Chromatography ◽  
Model System ◽  
Size Exclusion ◽  
Cyclic Polymers ◽  
Cyclic Polymer ◽  
System P ◽  
Exclusion Chromatography

Because cyclic polymers have intriguing physical properties, considerable synthetic strategies have been developed to create a wide variety of cyclic architectures.

Entrapment and release kinetics study of dyes from BSA microspheres forming a matrix and a reservoir system

2020 ◽  
Vol 8 (44) ◽  
pp. 10154-10161
Author(s):  
Kusha Sharma ◽  
Abed Saady ◽  
Avi Jacob ◽  
Ze’ev Porat ◽  
Aharon Gedanken
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ultrasonic Irradiation ◽  
Bovine Serum ◽  
Release Kinetics ◽  
Kinetics Study ◽  
Reservoir System ◽  
System P

Two kinds of Bovine Serum Albumin (BSA)-loaded microspheres were prepared in water-organic bilayer systems using ultrasonic irradiation.

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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