PROTEIN BINDING OF A SERIES OF RIFAMYCINS TO BOVINE SERUM ALBUMIN AS MEASURED BY GEL FILTRATION AND PARTITION DIALYSIS

Abstracts ◽  
1977 ◽  
pp. 133
Author(s):  
Alessandro Assandri ◽  
Luiqi Moro
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Bovine Serum ◽  
Gel Filtration

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

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

scholarly journals Acetyl-coenzyme A carboxylase from avocado (Persea americana) plastids and spinach (Spinacia oleracea) chloroplasts

1980 ◽  
Vol 187 (3) ◽  
pp. 667-676 ◽  
Author(s):  
S B Mohan ◽  
R G Kekwick
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spinacia Oleracea ◽  
Gel Filtration ◽  
Fold Increase ◽  
Persea Americana ◽  
Acetyl Coa ◽  
A Value

Preparations of acetyl-CoA carboxylase [acetyl-CoA-carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] have been obtained from the plastids of avocado (Persea americana) fruit mesocarp and from spinach (Spinacia oleracea) chloroplasts. Both preparations required bovine serum albumin, HCO3-, citrate and glycerol for stabilization. The molecular weight of the avocado enzyme was about 6.5 × 10(5) on the basis of 1 mol of biotin/mol of enzyme, the behaviour of both enzymes on gel filtration being in accord with such a value. Removal of the stabilizing bovine serum albumin resulted in the loss of a biotin-containing fragment from the avocado enzyme. Citrate stabilized the enzyme at 10 mM and activated it optimally at 3.0 mM, effecting an approx. 2-fold increase in Vmax. It is suggested that in vivo the enzyme may be located within the chloroplast lamellae.

scholarly journals The binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios

1974 ◽  
Vol 137 (3) ◽  
pp. 575-578 ◽  
Author(s):  
Geoffrey Allen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Bovine Serum ◽  
Equilibrium Dialysis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Weight Ratio ◽  
Binding Ratio ◽  
High Binding

The extent of binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios was investigated by gel filtration. The weight ratio of bound sodium dodecyl sulphate to bovine serum albumin increases with the NaCl concentration, and, except at low salt concentrations, with the concentration of sodium dodecyl sulphate. In the presence of 1.0g of sodium dodecyl sulphate/l, the binding ratio varied from 1.0 (at 0.04m-Na+) to 2.2 (at 0.44m-Na+). In the presence of 0.24m-Na+, the binding ratio increased with sodium dodecyl sulphate concentration, from 0.9 (0.2g of sodium dodecyl sulphate/l) to 2.0 (5g of sodium dodecyl sulphate/l), at 26°C, in a dilute sodium phosphate buffer. No significant dependence of the binding ratio upon temperature in the range 26–45°C was observed. These results differ from those of Reynolds & Tanford (1970a) obtained by equilibrium dialysis.

Casein Binds to the Cell Membrane and Induces Intracellular Calcium Signals in the Enteroendocrine Cell: A Brief Communication

2003 ◽  
Vol 228 (7) ◽  
pp. 850-854 ◽  
Author(s):  
Tohru Hira ◽  
Hiroshi Hara ◽  
Fusao Tomita ◽  
Yoritaka Aoyama
Keyword(s):  
Bovine Serum Albumin ◽  
Cell Membrane ◽  
Serum Albumin ◽  
Protein Binding ◽  
Calcium Channel ◽  
Intracellular Calcium ◽  
Dietary Protein ◽  
Bovine Serum ◽  
Enteroendocrine Cell ◽  
Resonance Sensor

Dietary protein but not amino acids stimulates cholecystokinin (CCK) secretion in rat mucosal cells. However, the dietary protein sensory mechanisms and the intracellular signal pathway in the enteroendocrine cells have not yet been clarified. The relationship between dietary protein binding to cell membrane and intracellular calcium responses were examined in the CCK-producing enteroendocrine cell line STC-1. The binding of solubilized STC-1 cell membrane to proteins was analyzed using a surface plasmon resonance sensor. Intracellular calcium concentrations of STC-1 cell suspensions loaded with Fura-2 AM were measured using a spectrafluorophotometer system with continuous stirring. Intracellular calcium concentrations in STC-1 cells were increased by exposure to α-casein or casein sodium, but not to bovine serum albumin. Solubilized STC-1 membranes bound to α-casein and casein sodium but did not bind to bovine serum albumin. α-Casein demonstrated higher membrane binding and intracellular calcium stimulating activities than casein sodium. Thus, protein binding to the STC-1 cell membrane and intracellular calcium responses were correlated. Intracellular calcium responses to α-casein were suppressed by an L-type calcium channel blocker. These results suggest that casein, a dietary protein, binds to a putative receptor on the CCK-producing enteroendocrine cell membrane and elicits the subsequent intracellular calcium response via an L-type calcium channel.

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