Recombinant Protein A Immobilized on Cross-linked Cellulose Microspheres for Immunoglobulin G Adsorption from Human Plasma

نویسندگان

  • Xiaodong Cao
  • Biyan Zhu
  • Tao Chen
  • Xufeng Zhang
  • Hua Dong
چکیده

Cross-linked cellulose microspheres (CL-CMs) were successfully prepared using an inverse crosslinking suspension method from a cellulose solution with sodium hydroxide/urea aqueous solution as a solvent and epichlorohydrin as the crosslinker. The effects of epichlorohydrin content on the appearance and dispersity, average pore volume, moisture content, and wet real density of CL-CMs were studied. The microspheres presented a good spherical shape and porous surface structure. After activation with NaIO4, the recombinant protein A was immobilized onto the surface of CL-CMs to form an immunoadsorbent. Adsorbents containing various amounts of protein A were applied to adsorb immunoglobulin G (IgG) from human plasma. The maximum IgG adsorption capacities with static adsorption and dynamic adsorption were 23 and 13 mg, respectively, per gram of CL-CMs carrying 6.8 mg of recombinant protein A. Therefore, CL-CMs immobilized with recombinant protein A have great potential for application in the field of blood purification.

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

Bioactivity Determination of Recombinant lysostaphin Immobilized on Glass Surfaces Modified by Cold Atmospheric Plasma on Staphylococcus aureus

Introduction: Staphylococcus aureus is a source of nosocomial infections and one of the significant concerns in patients with indwelling devices. Lysostaphin is a bacterially produced endopeptidase with a unique activity on S. aureus. Plasma, the fourth state of the material, consists of charged ions, free electrons, and activated neutral species. Biomedical applications of cold plasma are rapi...

متن کامل

Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...

متن کامل

Optimization of Enzymatic Synthesis of Ampicillin Using Cross-Linked Aggregates of Penicillin G Acylase

Penicillin G acylase from E. coli TA1 was immobilized by Cross-Linked Enzyme Aggregates (CLEA), a new method for immobilization. This biocatalyst and commercial immobilized penicillin G acylase (PGA-450) were used to study the effect of pH, temperature and substrate concentration on the synthesis of ampicillin from phenyl glycine methyl ester (PGME) and 6-aminopenicillanic acid (6-APA). Compare...

متن کامل

Generic method for attaching biomolecules via avidin-biotin complexes immobilized on films of regenerated and nanofibrillar cellulose.

We investigated the adsorption and chemical conjugation of avidin and its deglycosylated form, neutravidin, on films of regenerated and nanofibrillar cellulose. The dynamics and extent of biomolecular attachment were monitored in situ by quartz crystal microbalance microgravimetry and ex situ via surface analyses with atomic force microscopy and X-ray photoelectron spectroscopy. The installatio...

متن کامل

CLONING AND SEQUENCING OF A MITOCHONDRIAL AUTOANTIGEN WITH IMMUNOGLOBULIN G FROM PATIENTS WITH MULTIPLE SCLEROSIS

Multiple Sclerosis (MS) is a chronic neurological disease of the central nervous system (CNS), characterised by a cellular immune response in early stages and demyelination of the CNS later. Although the cause of MS is unknown, there is much evidence that points to MS as an autoimmune disease. To test the hypotheses that an Autoantigen is involved in MS, we screened a ?gt11 human foetal spinal ...

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:

دوره   شماره 

صفحات  -

تاریخ انتشار 2016