Penetrable silica microspheres for immobilization of bovine serum albumin and their application to the study of the interaction between imatinib mesylate and protein by frontal affinity chromatography

2015 ◽  
Vol 408 (3) ◽  
pp. 805-814 ◽  
Author(s):  
Liyun Ma ◽  
Jing Li ◽  
Juan Zhao ◽  
Han Liao ◽  
Li Xu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Affinity Chromatography ◽  
Imatinib Mesylate ◽  
Bovine Serum ◽  
Silica Microspheres ◽  
Frontal Affinity Chromatography

Adsorption of bovine serum albumin on superparamagnetic composite microspheres with a Fe3O4/SiO2 core and mesoporous SiO2 shell

RSC Advances ◽  
2015 ◽  
Vol 5 (126) ◽  
pp. 103760-103766 ◽  
Author(s):  
Xuemei Hou ◽  
Hongbo Xu ◽  
Lei Pan ◽  
Yanlong Tian ◽  
Xiang Zhang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Mesoporous Silica ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Silica Shell ◽  
Silica Microspheres ◽  
Composite Microspheres ◽  
Sio2 Shell ◽  
Mesoporous Silica Microspheres ◽  
Mesoporous Sio2

Magnetic sandwich structured mesoporous silica microspheres containing a silica-coated Fe3O4 core and a layered mesoporous silica shell have been successfully synthesized by multi-step reactions.

scholarly journals Studies of drug-protein binding by affinity chromatography. II. Interactions of bovine serum albumin with various ligands.

1979 ◽  
Vol 27 (9) ◽  
pp. 2048-2055 ◽  
Author(s):  
NAOMI I. NAKANO ◽  
TAKAYUKI OSHIO ◽  
NORIKO SATO ◽  
YOSHIMITSU SHIMAMORI ◽  
SHIGENORI YAMAGUCHI
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Affinity Chromatography ◽  
Bovine Serum ◽  
Drug Protein Binding

Estimation of interaction between polyanions and bovine serum albumin by means of affinity chromatography

1985 ◽  
Vol 30 (7) ◽  
pp. 2847-2852 ◽  
Author(s):  
Noriyuki Kuramoto ◽  
Munenori Sakamoto ◽  
Jiro Komiyama ◽  
Toshiro Iijima
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Affinity Chromatography ◽  
Bovine Serum

Role of terminal fucose residues in clearance of human glycosylated alpha-amylase

1988 ◽  
Vol 255 (3) ◽  
pp. G374-G381
Author(s):  
S. E. Tollefsen ◽  
J. L. Rosenblum
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Affinity Chromatography ◽  
Bovine Serum ◽  
Alpha Amylase ◽  
Lectin Affinity Chromatography ◽  
Lectin Affinity ◽  
Specific Receptors

Human glycosylated alpha-amylase contains a single biantennary N-linked oligosaccharide that terminates with the structure Fuc alpha 1,3(Gal beta 1,4)GlcNAc. To examine the role of terminal fucose in the clearance of alpha-amylase, we used lectin affinity chromatography to isolate an alpha-amylase fraction that contains two terminal fucoses (one in each branch of the oligosaccharide) and a fraction from which both terminal fucoses have been enzymatically removed. In the rat, the rate of clearance of the radioiodinated fraction with terminal fucoses is rapid (t1/2 = 12 min) and is slowed by mannosylated but not galactosylated bovine serum albumin. The rate of clearance of the radioiodinated alpha-amylase fraction with no terminal fucoses is also rapid (t1/2 = 9.5 min), but the clearance is now slowed by galactosylated bovine serum albumin. These findings indicate that the fucosylated and defucosylated alpha-amylase fractions are recognized by different carbohydrate-specific receptors. We conclude therefore that terminal fucose is the recognition marker that effects the physiological clearance of this glycoprotein.

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