Screening, Identification, and Potential Interaction of Active Compounds from Eucommia ulmodies Leaves Binding with Bovine Serum Albumin

2012 ◽  
Vol 60 (12) ◽  
pp. 3119-3125 ◽  
Author(s):  
Yuping Zhang ◽  
Mijun Peng ◽  
Liangliang Liu ◽  
Shuyun Shi ◽  
Sheng Peng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Potential Interaction ◽  
Active Compounds

scholarly journals Nrp1 is Activated by Konjac Ceramide Binding-Induced Structural Rigidification of the a1a2 Domain

Cells ◽  
2020 ◽  
Vol 9 (2) ◽  
pp. 517
Author(s):  
Seigo Usuki ◽  
Yoshiaki Yasutake ◽  
Noriko Tamura ◽  
Tomohiro Tamura ◽  
Kunikazu Tanji ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Intramolecular Interaction ◽  
Protein Secondary Structure ◽  
Potential Interaction ◽  
Activation Mechanism ◽  
Receptor Interaction ◽  
Intrinsically Disordered ◽  
Hydroxyl Fatty Acids

Konjac ceramide (kCer) is a plant-type ceramide composed of various long-chain bases and α-hydroxyl fatty acids. The presence of d4t,8t-sphingadienine is essential for semaphorin 3A (Sema3A)-like activity. Herein, we examined the three neuropilin 1 (Nrp1) domains (a1a2, b1b2, or c), and found that a1a2 binds to d4t,8t-kCer and possesses Sema3A-like activity. kCer binds to Nrp1 with a weak affinity of μM dissociation constant (Kd). We wondered whether bovine serum albumin could influence the ligand–receptor interaction that a1a2 has with a single high affinity binding site for kCer (Kd in nM range). In the present study we demonstrated the influence of bovine serum albumin. Thermal denaturation indicates that the a1a2 domain may include intrinsically disordered region (IDR)-like flexibility. A potential interaction site on the a1 module was explored by molecular docking, which revealed a possible Nrp1 activation mechanism, in which kCer binds to Site A close to the Sema3A-binding region of the a1a2 domain. The a1 module then accesses a2 as the IDR-like flexibility becomes ordered via kCer-induced protein rigidity of a1a2. This induces intramolecular interaction between a1 and a2 through a slight change in protein secondary structure.

scholarly journals Analysis of Bovine Serum Albumin Ligands fromPuerariae flosUsing Ultrafiltration Combined with HPLC-MS

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Ping Tang ◽  
Shihui Si ◽  
Liangliang Liu
Keyword(s):  
Natural Products ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
High Performance ◽  
Rapid Screening ◽  
Active Compounds ◽  
Fundamental Parameters ◽  
Isolation Techniques ◽  
Puerariae Flos

Rapid screening techniques for identification of active compounds from natural products are important not only for clarification of the therapeutic material basis, but also for supplying suitable chemical markers for quality control. In the present study, ultrafiltration combined with high performance liquid chromatography-mass spectrometry (HPLC-MS) was developed and conducted to screen and identify bovine serum albumin (BSA) bound ligands fromPuerariae flos. Fundamental parameters affecting the screening like incubation time, BSA concentration, pH, and temperature were studied and optimized. Under the optimum conditions, nine active compounds were identified by UV and MS data. The results indicated that this method was able to screen and identify BSA bound ligands form natural products without the need of preparative isolation techniques. Moreover, the method has more effective with easier operation procedures.

scholarly journals Antioxidant Activities of Centella asiatica Extract-loaded Bovine Serum Albumin Nanoparticles in Simulated Gastrointestinal System Study

2020 ◽  
Vol 141 ◽  
pp. 03001
Author(s):  
Kittiya Kesornbuakao ◽  
Patteera Chanapongpisan ◽  
Malinee Sriariyanun ◽  
Ir. Lindayani ◽  
Patchanee Yasurin
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Crude Extract ◽  
Bovine Serum ◽  
Antioxidant Activities ◽  
Centella Asiatica ◽  
Gastrointestinal System ◽  
Physical Parameters ◽  
Active Compounds ◽  
Albumin Nanoparticles

Bioavailability of active compounds extracted from herbs is generally limited to be adsorbed or expressed to target organisms due to several physical and chemical factors. Nanoparticle encapsulation techniques was developed to carry bioactive macromolecules of Centella asiatica (Buabok) in the form of C. asiatica Extract-loaded Bovine Serum Albumin Nanoparticles (CBNPs) to improve bioavailability. In this study, the antioxidant activities of CBNPs and C. asiatica crude extract were evaluated by using DPPH radical scavenging assay in the simulated gastrointestinal system, including mastication, stomach, duodenum, and ileum conditions to provide the environment which similar to in vivo system in terms of chemical and physical parameters. CBNPs were prepared by mixing of C. asiatica crude extract and BSA at different ratio of 1:2, 1:3, and 1:4. The results showed that the highest antioxidant activity of CBNP was observed when the ratio of crude extract and BSA at 1:2 was used at pH 2.0 or in the simulated stomach condition. The denaturation or unfolding of BSA in the simulated stomach occurred when pH was low could lead to the release of active compounds at certain area in gastrointestinal system.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

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.

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.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

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