Polyclonal antibody production against bovine serum albumin conjugated artemisinin in rabbit
نویسندگان
چکیده مقاله:
Abstract: The aim of the present study was to produce a polyclonal antibody against bovine serum albumin (BSA) conjugated with artemisinin. To gain an immunogenic character of artemisinin, a carboxyl group was added to it using mixed anhydride method. Then, the reactive compound of artemisinin was conjugated with BSA. The BSA+artemisinin were injected to white female New Zealand rabbits for two times. In the first injection, the Fraud's complete adjuvant was used, and two weeks later, a booster injection was carried out with a Fraud's incomplete adjuvant. Two weeks later, blood samples were collected; their serum were separated and frozen until assessment. The production of antibody against BSA+artemisinin was assayed by Immunoblot technique. Antibody was separated and concentrated by saturated ammonium sulfate. The assay confirmed the successful production of an antibody against BSA+artemisinin as a fundamental step in investigation of pharmacodynamics and pharmacokinetics of artemisinin. Key words: Artemisia sieberi, artemisinin, polyclonal antibody, BSA-conjugation
منابع مشابه
Peptide based polyclonal antibody production against bovine rotavirus non structure protein4 (NSP4)
The rotavirus nonstructural protein 4 (NSP4), is a multi functional protein that play key role in both viral morphogenesis and cytopathic effect associated with cell death. However, the complete biological effect of NSP4 remains to be clarified. Since to obtain further knowledge about this protein there is a need for recognizing antibody and there is no commercial antibody against this protein,...
متن کاملSerum Antibody to Bovine Serum Albumin I
To evaluate the re lat ionship be tween tumor burden and c i rculat ing immune complexes (IC) in ch i ldren with neurob lastoma (NBL), we studied sera col lected at intervals from pat ients with d isseminated (Stage III or IV) NBL. Sera from 10 of 12 pat ients conta ined IC by the Raji cell assay at some time dur ing the first 9 to 11 months of the study. H igher IC levels were observed in sera...
متن کاملDevelopment and characterization of polyclonal antibody against human kappa light chain in rabbit
Polyclonal antibodies against kappa light chain are used to diagnose diseases producing free light chain. The kappa and lambda light chains are products of immunoglobulin synthesis and released into the circulation in minor amounts such as serum, cerebrospinal fluid, urine and synovial fluid in normal condition. The purpose of this study was the production and purification of polyclonal immunog...
متن کاملFluorescein-conjugated Bovine Albumin
Fluorescein-bovine albumin conjugates have been prepared and found not to differ appreciably in size, shape, and homogeneity from the precursor, bovine serum albumin. Fluorescein has also been conjugated to rat plasma proteins. Their disappearance rates from the circulation of rats correspond with those obtained from the use of isotope labeling. Their sites of localization in rat tissues were s...
متن کاملThiol-reactive clenbuterol analogues conjugated to bovine serum albumin.
Several novel thiol-reactive clenbuterol analogues were coupled in high yield with bovine serum albumin (BSA). After labelling of unreacted cysteines with maleimide spin label (MiSL), the yield of the coupling reaction was determined by electron paramagnetic resonance (EPR) spectroscopy and spectral analysis. Two spin-probe populations with different mobility states were quantitatively determin...
متن کاملFluorescence dynamics of bovine serum albumin (BSA) conjugated CdZnS nanocrystallites
We report on the production of composite semiconductor CdZnS nanoparticles by adopting an inverse micellar route, using bis (2-ethylhexyl) sulfosuccinate (aerosol-AOT) as surfactant and with a degree of hydration w0 = [H2O] : [AOT] = 8.9. Prior to bioconjugation (conjugation with bovine serum albumin (BSA)), the hydrophobic surface of the nanocrystals were made hydrophilic with thiol treatment ...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ذخیره در منابع من قبلا به منابع من ذحیره شده{@ msg_add @}
عنوان ژورنال
دوره 2 شماره 2
صفحات 87- 94
تاریخ انتشار 2008-10-01
با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.
کلمات کلیدی
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023