Eukaryotic ribosomal proteins: the number of proteins in the subunits and their isoelectric points.

نویسندگان

  • Huynh-Van-Tan
  • M Gavrilovic
  • G Schapira
چکیده

Today the number of proteins [l-5] in eukaryotic ribosomal subunits as well as their molecular weights [6] are fairly well determined. Many of these proteins are also isolated and purified [3]. Just like histones, ribosomal proteins are very basic. Both kinds occur naturally in combination with nucleic acids: so it is likely that electrical charges play an important part in the association of these proteins to their respective nucleic acids. As a step towards the understanding of this association it seems therefore necessary to evaluate the electrical charges on the proteins. This may be done globally by measuring their isoelectric points. As the isolation of individual ribosomal proteins is an elaborate and time consuming process, the two-dimensional electrophoresis method of Kaltschmidt [7], which does not require isolation of individual proteins, is used to this end.

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

Effect of 8 Weeks of Endurance Training on S6K1 and 4EBP1 Proteins Content in the Left Ventricle of the Heart of Diabetic Rats Induced by Streptozotocin and Nicotinamide

Introduction: Physiological hypertrophy of the heart is dependent on cellular pathways and important proteins such as the ribosomal protein S6 kinase beta-1 (S6K1) and  eukaryotic translation intiation factor4E-binding protein-1(4EBP1). The aim of this study was to investigate the effect of 8 weeks of endurance training on ribosomal protein S6 kinase beta-1 and eukaryotic translation initiation...

متن کامل

A Novel Vector for Expression/Secretion of Properly Folded Eukaryotic Proteins: a Comparative Study on Cytoplasmic and Periplasmic Expression of Human Epidermal Growth Factor in E. coli

Expression of eukaryotic proteins in E. coli often results in their aggregation. Proper folding and solubility of therapeutical proteins are the pre-requisite for their bioactivity. This is not achieved in cytoplasmic expression in E. coli because of the absence of disulfide bonds formation. A novel expression/secretion vector was constructed which exploited β-lactamase signal sequence to trans...

متن کامل

Designing and Development of a DNA Vaccine Based On Structural Proteins of Hepatitis C Virus

Background: Hepatitis C virus (HCV) infection is one of the most prevalent infectious diseases responsible for high morbidity and mortality worldwide. Therefore, designing new and effective therapeutics is of great importance. The aim of the current study was to construct a DNA vaccine containing structural proteins of HCV and evaluation of its expression in a eukaryot...

متن کامل

Selecting appropriate hosts for recombinant proteins production: Review article

In recent years, the number of recombinant proteins used for therapeutic applications and industry has increased dramatically. Recombinant proteins are produced in many host organisms (microbial, insect, plant and mammalian cells). There are many factors to consider when choosing the optimal system for protein expression and purification including the mass, purity or solubility of the recombina...

متن کامل

Assessment of seed storage protein composition of six Iranian adopted soybean cultivars [Glycine max (L.) Merrill.]

Seed protein quality is an important topic in the production of soybean. The quality of soybean proteins is limited by anti-nutrient proteins and low levels of essential sulfur amino acids. In this study, protein content and solubility of six cultivars were evaluated and seed storage proteins were analyzed using SDS-PAGE and scanning densitometry. The results showed that seed storage protein ba...

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:
  • FEBS letters

دوره 45 1  شماره 

صفحات  -

تاریخ انتشار 1974