Site accessibility and the pH dependence of the saturation capacity of a highly cross-linked matrix Immobilized metal affinity chromatography of bovine serum albumin on chelating superose

1997 ◽  
Vol 767 (1-2) ◽  
pp. 11-23 ◽  
Author(s):  
Anshuman V. Patwardhan ◽  
Mohammad M. Ataai
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Affinity Chromatography ◽  
Bovine Serum ◽  
Ph Dependence ◽  
Immobilized Metal Affinity Chromatography ◽  
Metal Affinity ◽  
Saturation Capacity

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.

Adsorption of the Polyvinylidene Fluoride-Based Metal Affinity Membrane towards Bovine Serum Albumin

2015 ◽  
Vol 1083 ◽  
pp. 3-8
Author(s):  
Xiu Li Wang ◽  
Fan Zhang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Polyvinylidene Fluoride ◽  
Metal Affinity ◽  
Adsorption Performance ◽  
Affinity Membrane ◽  
Affinity Membranes

Three kinds of polyvinylidene fluoride (PVDF)-based immobilized metal affinity membranes (IMAM), namely, Cu (II)-IMAM, Co (II)-IMAM and Ni (II)-IMAM were prepared to recover bovine serum albumin (BSA) from the solutions. Adsorption of the aforementioned membranes towards BSA were studied with the presence of Ca (II) and PO43–. The adsorption performance of the membranes followed the order of Co (II)-IMAM > Cu (II)-IMAM > Ni (II)-IMAM. The existent PO43– exhibited a larger interference on BSA uptake than Ca (II).

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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