Immunogenic comparison of two coupling methods of marine polysaccharide to bovine serum albumin.

نویسندگان

  • Li Gan
  • Xianliang Xin
  • Meiyu Geng
  • Jian Ding
چکیده

Two conjugates of marine polysaccharide (MPS) and bovine serum albumin (BSA) were prepared using two methods, periodate oxidation and reductive amination, with the intent of enhancing its immunogenicity. Sera samples from Balb/c mice immunized with the products named MPS-BSAp and MPS-BSAr respectively were evaluated by enzyme-linked-immunosorbent assay (ELISA). The results showed that mice immunized with MPS-BSAp produced antibodies not against MPS but rather against MPS-BSAp, while the mice immunized with MPS-BSAr produced high titer antibodies only specific for MPS. The difference was attributed to the fact that the epitopes of MPS had been changed in the coupling process by periodate oxidation. A mouse immunized with MPS-BSAr was chosen to prepare monoclonal antibodies (mAbs) specific for polysaccharide MPS. A hybridoma cell line that secreted monoclonal antibody recognizing specifically polysaccharide MPS was established.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Polyclonal antibody production against bovine serum albumin conjugated artemisinin in rabbit

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...

متن کامل

Targeted Delivery of 5-fluorouracil with Monoclonal Antibody Modified Bovine Serum Albumin Nanoparticles

Herein, 1F2, an anti-HER2 monoclonal antibody (mAb), was covalently coupled to the surface of 5-Fluorouracil (5-FU) loaded bovine serum albumin (BSA) nanoparticles. Concerning two different crosslinkers for conjugation of 1F2, Maleimide-poly (ethylene glycol)-Succinimidyl carbonate (Mal-PEG5000-NHS) was selected due to its higher conjugation efficiency (23±4 %) obtained in comparison to N-succi...

متن کامل

Targeted Delivery of 5-fluorouracil with Monoclonal Antibody Modified Bovine Serum Albumin Nanoparticles

Herein, 1F2, an anti-HER2 monoclonal antibody (mAb), was covalently coupled to the surface of 5-Fluorouracil (5-FU) loaded bovine serum albumin (BSA) nanoparticles. Concerning two different crosslinkers for conjugation of 1F2, Maleimide-poly (ethylene glycol)-Succinimidyl carbonate (Mal-PEG5000-NHS) was selected due to its higher conjugation efficiency (23±4 %) obtained in comparison to N-succi...

متن کامل

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 کامل

I an Immunological Approach for Ctx

The application of immunological techniques for the detection of low molecular weight, nonimmunogenic compounds has increased markedly in the past decade. The ability to conjugate these haptenic small molecules covalently to appropriate immunogenic carriers via their functional groups has led to the production of specific antibodies to the haptenic molecules following administration into approp...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Biological & pharmaceutical bulletin

دوره 27 10  شماره 

صفحات  -

تاریخ انتشار 2004