Stimuli-responsive nanoparticles by thermal treatment of bovine serum albumin inside its complexes with chondroitin sulfate

2019 ◽  
Vol 87 ◽  
pp. 602-610 ◽  
Author(s):  
Aristeidis Papagiannopoulos ◽  
Eleni Vlassi
2007 ◽  
Vol 361-363 ◽  
pp. 127-130 ◽  
Author(s):  
Elena Mavropoulos ◽  
Nilce C.C. da Rocha ◽  
Maria Helena M. Rocha-Leão ◽  
Antonella M. Rossi

Adsorption experiments of bovine serum albumin on hydroxyapatite previously annealed at temperatures up to 1100°C was performed at 37°C and phosphate buffer, pH 6.0. Kinetic process was very efficient and irreversible for low phosphate buffer concentration. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HA specific surface area and the number of surface active sites. However, it was verified that particle size was also an important parameter for bovine serum albumin immobilization.


2017 ◽  
Vol 58 (3-4) ◽  
pp. 276-285 ◽  
Author(s):  
Nilotpal Barooah ◽  
Raman Khurana ◽  
Achikanath C. Bhasikuttan ◽  
Jyotirmayee Mohanty

2007 ◽  
Vol 330-332 ◽  
pp. 1009-1012 ◽  
Author(s):  
Hajime Watanabe ◽  
Toshiyuki Ikoma ◽  
Guo Ping Chen ◽  
M. Tanaka

Time-controlled releases of proteins from hydroxyapatite/chondroitin sulfate (HAp/ChS) spherical microparticles were achieved by the addition of zinc cation into the mixture solutions of HAp/ChS and protein as a novel formulation. The initial bursts of proteins, such as cytochrome c and bovine serum albumin, were apparently suppressed by the amount of zinc cation, which could be attributed to the formation of coordinate bonds of zinc cation among proteins and/or ChS moleculars. The increase of molecular lengths of ChS chains decreased the adsorbed amount of proteins, which did not apparently affected to the release of proteins.


Author(s):  
G. D. Gagne ◽  
M. F. Miller

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.


Sign in / Sign up

Export Citation Format

Share Document