scholarly journals 2P-007 Protective Effect of Gemini Surfactant on Secondary Structural Change of Bovine Serum Albumin in Thermal Denaturation up to 130℃(Protein:Structure,The 47th Annual Meeting of the Biophysical Society of Japan)

2009 ◽  
Vol 49 (supplement) ◽  
pp. S107
Author(s):  
Yoshiko Moriyama ◽  
Yuu Tanizaki ◽  
Hironori Harano ◽  
Kunio Takeda
Keyword(s):  
Structural Change ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Annual Meeting ◽  
Bovine Serum ◽  
Thermal Denaturation ◽  
Gemini Surfactant ◽  
Biophysical Society ◽  
Secondary Structural Change

scholarly journals 3P-006 Additive Effect of Surfactant on the Structural Change of Bovine Serum Albumin at High Temperatures(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S128
Author(s):  
Yoshiko Moriyama ◽  
Hironori Harano ◽  
Etsuo Inui ◽  
Emi Watanabe ◽  
Kentaro Kobayashi ◽  
...  
Keyword(s):  
Structural Change ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Annual Meeting ◽  
High Temperatures ◽  
Bovine Serum ◽  
Additive Effect ◽  
Biophysical Society

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

Albumin reduces basement membrane hydraulic conductance in part due to arginyl side groups

1995 ◽  
Vol 269 (5) ◽  
pp. H1514-H1521 ◽  
Author(s):  
M. A. Katz ◽  
M. L. La Marche
Keyword(s):  
Extracellular Matrix ◽  
Bovine Serum Albumin ◽  
Basement Membrane ◽  
Serum Albumin ◽  
Protective Effect ◽  
Binding Sites ◽  
Bovine Serum ◽  
Hydraulic Conductance ◽  
Experimental Control ◽  
Low Concentrations

Albumin reduces capillary hydraulic conductance (Lp) even at low concentrations. To determine if part of this barrier protective effect might be extracellular, we studied the effects of bovine serum albumin (BSA) on Lp of self-assembled basement membrane (Matrigel). Lp with tris(hydroxymethyl)aminomethane (Tris) buffer superfusate was stable at 1.77 +/- 0.22 x 10(-5) (SE) cm.s-1.cmH2O-1 over several hours. At 0.1 g/dl BSA, experimental/control (Tris) Lp fell to 83.1 +/- 6.0% (2P < 0.025), with decreases to 72.4 +/- 3.7% at 1 g/dl (2P < 0.005), 45.3 +/- 5.1% at 2.5 g/dl (2P < 0.001), and 45.0 +/- 4.8% at 4.0 g/dl (2P < 0.001). In separate experiments, BSA arginine groups were neutralized by 1,2-cyclohexanedione (CHD), and experimental/control Lp values were measured. At 2.5 g/dl, CHD-BSA depressed Lp to 54.4 +/- 4.8%, while unmodified BSA reduced Lp to 40.8 +/- 3.5% of Tris control (2P = 0.05). Finally, soluble arginine at three- and sixfold the arginine in BSA was added to BSA superfusate. For threefold, Lp rose to 120 +/- 8% of BSA level and for sixfold to 129 +/- 9% (2P < 0.05). We conclude that some part of the albumin protective effect is very likely due to consequences on extracellular matrix and that at least 18-22% of this effect is related to arginine groups on albumin when computed from Lp, and up to 34% when viscosity is taken into account. Membrane-saturable arginine-binding sites can be unbound with arginine, thus nullifying part of the barrier protective effect of BSA.

Interactions between bovine serum albumin and gemini surfactant alkanediyl-α, ω-bis(dimethyldodecyl-ammonium bromide)

Biopolymers ◽  
2006 ◽  
Vol 83 (3) ◽  
pp. 243-249 ◽  
Author(s):  
Yingying Pi ◽  
Yazhuo Shang ◽  
Changjun Peng ◽  
Honglai Liu ◽  
Ying Hu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Gemini Surfactant ◽  
Ammonium Bromide

Thermal denaturation of bovine serum albumin and its oligomers and derivativespH dependence

1995 ◽  
Vol 45 (6) ◽  
pp. 1255-1264 ◽  
Author(s):  
G. Barone ◽  
S. Capasso ◽  
P. Del Vecchio ◽  
C. De Sena ◽  
D. Fessas ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Denaturation

Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study

2014 ◽  
Vol 49 (4) ◽  
pp. 623-630 ◽  
Author(s):  
Muzaffar Ul Hassan Mir ◽  
Jitendra Kumar Maurya ◽  
Shahnawaz Ali ◽  
Shah Ubaid-ullah ◽  
Abbul Bashar Khan ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Molecular Interaction ◽  
Bovine Serum ◽  
Gemini Surfactant ◽  
Docking Study ◽  
Molecular Docking Study ◽  
Cationic Gemini Surfactant

Investigation of thermal denaturation of solid bovine serum albumin by terahertz dielectric spectroscopy

2013 ◽  
Vol 1049 ◽  
pp. 441-445 ◽  
Author(s):  
Xiangjun Li ◽  
Xiuhua Fu ◽  
Jianjun Liu ◽  
Yong Du ◽  
Zhi Hong
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Dielectric Spectroscopy ◽  
Bovine Serum ◽  
Thermal Denaturation
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