Gel-Filtration Chromatography.
نویسندگان
چکیده
Gel-filtration chromatography is a versatile method that permits the effective separation of biological molecules in high yield. This article describes the basis of the method, the selection of suitable operating conditions, and contrasts typical matrix types. Applications of the technique are described, with references to the scientific literature.
منابع مشابه
Comparison of two gel filtration chromatography resins for the purification of foot-and-mouth disease virus as a purified vaccine antigen
Introduction: Foot-and-mouth disease (FMD) is a highly contagious and economically devastating viral disease of livestock that is categorized in list A of animal diseases by the World Organisation for Animal Health (OIE). Vaccination is effective against FMD and the vaccine production centers largely use the industrial ultra-filtration and chromatography in order to remove the cellular proteins...
متن کاملRole of Molecular Interactions and Oligomerization in Chaperone Activity of Recombinant Acr from Mycobacterium tuberculosis
Background: The chaperone activity of Mycobacterium tuberculosis Acr is an important function that helps to prevent misfolding of protein substrates inside the host, especially in conditions of hypoxia. Objectives: The aim of this study was to establish the correlation of structure and function of recombinant Acr proteins both before and after ge...
متن کاملPurification and characterisation of gelonin from seeds of Gelonium multiflorum.
Gelonin, a ribosome-inactivating protein has been isolated from the seeds of Gelonium multifluorum of Euphorbiaceae family by two methods and the results are compared. In method-I conventional aqueous extraction, cation-exchange and gel-filtration chromatography has been used. In method-II S-Sepharose fast flow gel has been used to purify the proteins from the seed extract, followed by ammonium...
متن کاملPurification of tonin by affinity chromatography.
Tonin has been purified from rat submaxillary glands. The purification procedure included affinity chromatography on Sepharose 4B coupled to antitonin followed by DEAE chromatography and gel filtration on Sephadex G-100. Homogeneity of the purified enzyme was confirmed by Sephadex G-100 gel filtration, disc electrophoresis, and isoelectric focusing on polyacrylamide gel, immunodiffusion, and im...
متن کاملA novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa.
A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was u...
متن کاملISOLATION AND PURIFICATION OF RIBOFLAVIN BINDING PROTIEN FROM COOT EGG-YOLK (Fulica atra)
Riboflavin-binding protein (RfBP) was isolated, purified and characterized from Coot (Fulica atra) egg. The RfBP was purified using DEAE-Sepharose ion exchange chromatography followed by gel filtration on Sephadex G-100. The purity of the proteins was judged by SDSPAGE. The protein migrated as a single band on SDS gel with a molecular weight of corresponding to nearly 29 Kd.
متن کاملذخیره 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 ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Methods in molecular biology
دوره 1485 شماره
صفحات -
تاریخ انتشار 2011