In vitro binding of dantrolene to bovine serum albumin and rabbit red blood cell ghosts

1982 ◽  
Vol 60 (10) ◽  
pp. 1307-1311 ◽  
Author(s):  
A. R. Dehpour ◽  
M. Mahmoudian
Keyword(s):  
Bovine Serum Albumin ◽  
Blood Cell ◽  
Serum Albumin ◽  
Red Blood Cell ◽  
Binding Sites ◽  
Blood Cells ◽  
Bovine Serum ◽  
Association Constant ◽  
Dantrolene Sodium

The binding of dantrolene to rabbit red blood cell (RBC) ghosts and bovine serum albumin as models of receptor sites was studied using fluorescence techniques. Dantrolene upon binding to rabbit RBC ghosts and bovine serum albumin showed fluorescence with emission maxima at 495 and 500 nm, respectively. Dantrolene bound to rabbit RBC ghosts with an association constant of 6.06 × 104 M−1 and there were 2.4 × 106 dantrolene binding sites per ghost. The binding of dantrolene to bovine serum albumin showed an anomaly with respect to dantrolene concentration. Dantrolene at concentrations of 1.25 – 3.75 μM bound to bovine serum albumin with an association constant of 1.72 × 104 M−1 and there were 1.078 binding sites/mol bovine serum albumin. The higher affinity of dantrolene toward blood cells was confirmed by studying the distribution of dantrolene between blood cells and plasma after a single i.p. injection of dantrolene sodium (3 mg/kg) to albino rabbits. It was found that the concentration of dantrolene in rabbit blood cells was 2.76 times that of plasma.

Bovine serum albumin bioconjugated graphene oxide: Red blood cell adhesion and hemolysis studied by QCM-D

2015 ◽  
Vol 356 ◽  
pp. 844-851 ◽  
Author(s):  
Bing Cai ◽  
Kebang Hu ◽  
Chunming Li ◽  
Jing Jin ◽  
Yuexin Hu
Keyword(s):  
Graphene Oxide ◽  
Cell Adhesion ◽  
Bovine Serum Albumin ◽  
Blood Cell ◽  
Serum Albumin ◽  
Red Blood Cell ◽  
Bovine Serum

scholarly journals In vitro Model for Studying Interactions between Ketorolac and Omeprazole with Bovine Serum Albumin by UV-Spectroscopic Method

2015 ◽  
Vol 17 (1) ◽  
pp. 92-98 ◽  
Author(s):  
Kanij Nahar Deepa ◽  
Md Khalid Hossain ◽  
Md Shah Amran ◽  
Shaila Kabir
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Site ◽  
Bovine Serum ◽  
Association Constant ◽  
Spectroscopic Method ◽  
Free Fraction ◽  
In Vivo Model ◽  
Specific Probe

The binding of Ketorolac and Omeprazole to bovine serum albumin (BSA) was studied by equilibrium dialysis method followed by UV spectroscopy. Warfarin and Diazepam were used as site-I and site-II specific probe, respectively. The binding of Ketorolac and Omeprazole was characterized by two sets of association constant: high affinity association constant (K1) with low capacity binding site (n1) and low affinity association constant (K1) with high capacity binding site (n1). In this study, n1 and n1 values were found to be 0.25 ± 0.006 and 1.8 ± 0.025 for Ketorolac and 0.22 ± 0.030 and 1.3±0.035 for Omeprazole at pH 7.4 and 37°C, respectively. At the same condition, the values of K1 and K1 for Ketorolac were found to be 0.624 ± 0.033 ?M-1 and 0.133 ± 0.023 ?M-1 and that of Omeprazole were 0.51 ± 0.001 ?M-1 and 0.28 ± 0.005 ?M-1, respectively. Site specific probe displacement studies implied that both Ketorolac and Omeprazole bind predominantly to site-II, the Diazepam site. In the present study, both Ketorolac and Omeprazole increased the free fraction of each other when they simultaneously bound to BSA. They compete for a common binding site on the albumin molecule, thereby free fraction of both the drugs was increased as compared to the level obtained when the drugs were given individually. We, thus, conclude that during concurrent administration of Ketorolac and Omeprazole adequate precautions should be taken. However, further studies are needed on in-vivo model to substantiate the findings from in-vitro experiments. DOI: http://dx.doi.org/10.3329/bpj.v17i1.22323 Bangladesh Pharmaceutical Journal 17(1): 92-98, 2014

Effect of Bovine Serum Albumin on Red Blood Cell Optical Anisotropy Probed Through the Optomechanical Response in an Optical Trap

2017 ◽  
Vol 376 (1) ◽  
pp. 1600209
Author(s):  
Parthasarathi Praveen ◽  
Selvan Rekha ◽  
Devarkonda Chetana ◽  
Shruthi S. Iyengar ◽  
Sarbari Bhattacharya ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Blood Cell ◽  
Serum Albumin ◽  
Red Blood Cell ◽  
Bovine Serum ◽  
Optical Anisotropy ◽  
Optical Trap

Pregnancy-blocking progesterone antibody targets specifically the uterus through its progesterone-binding sites

1990 ◽  
Vol 4 (3) ◽  
pp. 283-291 ◽  
Author(s):  
M.-W. Wang ◽  
A. Whyte ◽  
R. B. Heap ◽  
M. J. Taussig
Keyword(s):  
Monoclonal Antibody ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Passive Immunization ◽  
Uterine Epithelium ◽  
High Affinity ◽  
Specific Targeting

ABSTRACT Passive immunization with a mouse monoclonal antibody against progesterone, designated DB3, blocks pregnancy in several species. We have previously reported that DB3 localizes in the mouse uterine epithelium shortly before normal implantation. This phenomenon is pregnancy dependent and specific for the progesterone antibody. In this study we demonstrate that DB3 is present in the lumen of the uterus 36 h after an i.p. injection; this correlates with the time of maximum antibody reaction on the uterine epithelium. Incubation of DB3 with free progesterone, progesterone-hemisuccinate or progesterone—bovine serum albumin before administration prevented its localization on the epithelium, indicating that the localization requires free progesterone-binding sites and thus probably depends upon progesterone binding. In addition, studies in vitro show that DB3 can effectively bind to progesterone carried by high-affinity progesterone-binding protein purified from coypu plasma. We suggest that specific targeting of DB3 may be through progesterone associated with a progesterone-binding molecule on the membrane of the uterine epithelia. This may be an important part of the mechanism of antibody action against implantation.

Sensitive Radioimmunoassay for Detection of O6-Ethyldeoxyguanosine in D N A Exposed to the Carcinogen Ethylnitrosourea in vivo or in vitro

1978 ◽  
Vol 33 (11-12) ◽  
pp. 897-901 ◽  
Author(s):  
Rolf Müller ◽  
Manfred F Rajewsky
Keyword(s):  
Nucleic Acid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Association Constant ◽  
High Specificity ◽  
Diploid Cell ◽  
Molar Ratio

O8-ethyl-2′-deoxyguanosine (O8-EtdGuo) is a major premutational product formed in both in­tracellular DNA and in purified DNA in vitro, after exposure to the potent alkylating carcinogen N-ethyl-N-nitrosourea (EtNU). Antibodies directed against O8-EtdGuo were obtained by immunizing rabbits with a conjungate of O6-EtGuo and bovine serum albumin. In a competitive radioimmuno­assay (RIA), with O8-Et[8,5′·3H]dGuo as a tracer and various alkylated and natural nucleic acid components as inhibitors, these antibodies show high specificity for O6-EtdGuo and detect this product at a level of 0.3 picomol (antibody association constant, 7×108l/mol). In a sample of 130 μg of hydrolyzed DNA, O6-EtdGuo can thus be measured at a molar ratio of O8-EtdGuo/2′- deoxyguanosine of about 3×10-8, i. e., about 5×103 O8-EtdGuo molecules per diploid cell. Exam­ples are given for the quantitation of Oe-EtdGuo in DNA exposed to EtNU in vivo or in vitro.

Exploration of Fungal Lipase as Direct Target of Eugenol through Spectroscopic Techniques

2019 ◽  
Vol 26 (12) ◽  
pp. 919-929
Author(s):  
Farheen Naz ◽  
Haider Anis ◽  
Ziaul Hasan ◽  
Asimul Islam ◽  
Luqman A. Khan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Structural Changes ◽  
Tertiary Structure ◽  
Spectroscopic Techniques ◽  
Vis Spectroscopy ◽  
Direct Target

Background:Fungal lipase dependent processes are important for their pathogenicity. Lipases can therefore be explored as direct target of promising herbal antifungals.Objective:We explored Aspergillus niger lipase as a direct target of eugenol through spectroscopic techniques and compare results with Bovine Serum Albumin and lysozyme to comment on selectivity of eugenol towards lipase.Methods:In vitro activity assays of lipase are used to determine concentration ranges. UV-Visible, Fluorescence and Circular dichroism spectroscopy were employed to determine binding constant, stoichiometric binding sites and structural changes in Lipase, BSA and lysozyme following incubation with varying concentrations of eugenol.Results:In activity assays 50% inhibition of lipase was obtained at 0.913 mmoles/litre eugenol. UV-vis spectroscopy shows formation of lipase-eugenol, Bovine Serum Albumin-eugenol and lysozyme-eugenol complex well below this concentration of eugenol. Eugenol binding caused blue shift with Bovine Serum Albumin and lysozyme suggestive of compaction, and red shift with lipase. Negative ellipticity decreased with lipase but increased with Bovine Serum Albumineugenol and lysozyme-eugenol complexes suggesting loss of helical structure for lipase and compaction for Bovine Serum Albumin and lysozyme. Binding of eugenol to lipase was strong (Ka= 4.7 x 106 M-1) as compared to Bovine Serum Albumin and lysozyme. The number of stoichiometric eugenol binding sites on lipase was found to be 2 as compared to 1.37 (Bovine Serum Albumin) and 0.32 (lysozyme). Docking results also suggest strong binding of eugenol with lipase followed by Bovine Serum Albumin and lysozyme.Conclusion:Eugenol is found to be effective inhibitor and disruptor of secondary and tertiary structure of lipase, whereas its binding to Bovine Serum Albumin and lysozyme is found to be weak and less disruptive of structures suggesting selectivity of eugenol towards lipase.

A Precipitin-like Reaction of the Hemolymph of the Lobster Homarus americanus

1969 ◽  
Vol 26 (5) ◽  
pp. 1392-1397 ◽  
Author(s):  
James E. Stewart ◽  
Diane M. Foley
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Serum Proteins ◽  
Homarus Americanus ◽  
Test Period ◽  
Fluorescent Material

The levels of fluorescent material in the hemolymph of lobsters injected with serum proteins from lobster hemolymph labelled with fluorescein remained relatively constant over a 6-day test period; the levels in lobsters injected with bovine serum albumin labelled with fluorescein declined rapidly. A precipitin-like reaction was observed when lobster hemolymph serum was titrated with bovine serum albumin in vitro.

Preparation and in vitro photodynamic activities of novel axially substituted silicon (IV) phthalocyanines and their bovine serum albumin conjugates

2006 ◽  
Vol 16 (9) ◽  
pp. 2450-2453 ◽  
Author(s):  
Xiong-Jie Jiang ◽  
Jian-Dong Huang ◽  
Yu-Jiao Zhu ◽  
Fen-Xiang Tang ◽  
Dennis K.P. Ng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum
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