The chromatography of growth hormone on cellulose derivatives.

نویسندگان

  • S ELLIS
  • M E SIMPSON
چکیده

In this paper a report is made of the chromatographic behavior of growth hormone on columns of carboxymethylcellulose and diethylaminoethylcellulose. Ion exchange chromatography on the synthetic resin, Amberlite IRC-50, has been utilized to purify and to assess the homogeneity of a number of proteins. This resin has been used in chromatographic studies on cytochrome c (l), ribonuclease (2), lysozyme (3), chymotrypsin o( (4), and sheep fetal CO hemoglobin and bovine hemoglobin (5). Recently, certain derivatives of cellulose possessing ion exchange groups have also been studied with regard to the fractionation of proteins. Peterson and Sober have published reports on the use of columns of carboxymethylcellulose and diethylaminoethylcellulose in the fractionation of plasma proteins (6, 7) and of enzymes (8). Although the details of the preparation of the adsorbents which they used (9) have become available since the present study was completed, a brief description of the preparation of cellulose derivatives is included in this paper. This is desirable, since differences exist in the conditions of preparation such as concentration, temperature, and reaction time, which may affect the adsorption properties of the resulting cellulose derivatives.

برای دانلود رایگان 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

Persian sturgeon growth hormone elaboration and purification

In this study Escherichia coli DE3 containing expression vector (pET21a) with cloned Persian sturgeon growth hormone (psGH) gene was grown in 10 mL LB broth on a 150 rpm shaker, at the temperature of 37 °C. At the late log phase (determined by OD standard curve) 100 &muL isopropyl &beta-D-1-thiogalactopyranoside (IPTG) was added for induction of GH synthesis. Samples were taken every 2 hours an...

متن کامل

Persian sturgeon growth hormone elaboration and purification

In this study Escherichia coli DE3 containing expression vector (pET21a) with cloned Persian sturgeon growth hormone (psGH) gene was grown in 10 mL LB broth on a 150 rpm shaker, at the temperature of 37 °C. At the late log phase (determined by OD standard curve) 100 &muL isopropyl &beta-D-1-thiogalactopyranoside (IPTG) was added for induction of GH synthesis. Samples were taken every 2 hours an...

متن کامل

[The effect of iodination on the biological and immunological activities of the human growth hormone and prolactin].

The human growth hormone (hGH) and human prolactin (hPRL) were iodinated with 125I using the lactoperoxidase method and purified by gel filtration on a Sephadex G-100 column and by ion exchange chromatography on a diethyl-aminoethyl (DEAE) cellulose column. Aliquots of the peak fraction on the Sephadex G-100 column and each fraction on the DEAE cellulose column were tested by radioimmunoassay (...

متن کامل

Increased Production and Activity of Cellulase Enzyme of Trichoderma reesei by Using Gibberellin Hormone

Cellulolytic complex are enzymes capable of hydrolyzing cellulose. Due to rapid growth in population and industrialization, most countries are required to produce more fuel. Production of bioethanol from lignocellulosic biomass is very challenging due to environmental pollution by fossil fuels. Cellulases play a significant role in biotechnological processes. The cost of production of cellulase...

متن کامل

Diethylenetriamine supported on cellulose as a biodegradable and recyclable basic heterogeneous catalyst for the synthesis of spirooxindole derivatives

In the present study, the synthesis of diethylene triamine supported on cellulose biopolymer as a biodegradable solid basic heterogeneous catalyst was suggested. Then, the applicability of the synthesized catalyst cellulose bonded N-propyl diethylene triamine (CBPDETA) was tested for the synthesis of oxindole derivatives, an important class of potentially bioactive compounds. A various series o...

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

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 220 2  شماره 

صفحات  -

تاریخ انتشار 1956