Isolation of Streptolysin O by Preparative Polyacrylamide Gel Electrophoresis
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چکیده
منابع مشابه
Purification of horse serum cholinesterase by preparative polyacrylamide gel electrophoresis.
Preparative polyacrylamide gel electrophoresis has been used in the final stages of purification to prepare horse serum cholinesterase which was at least 9.5% pure, as judged by analytical polyacrylamide gel electrophoresis. The starting material, already purified about 109-fold by the Strelitz method, was purified an additional 89-fold by the procedure. The method involved Sephadex G-ZOO and S...
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Preparative polyacrylamide gel electrophoresis has been used to purify the enterotoxin of Clostridium perfringens from Sephadex G-100 extracts. Purified toxin of high specific activity was eluted in 1 to 3 h, depending upon the length of the acrylamide gel used. Recovery of biological activity with this technique ranged from 80 to 90%. The purity and physical characteristics of the toxin were s...
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1. Human growth hormone was prepared from acetone-dried residues after extraction of gonadotrophins from pituitary glands. 2. Crude growth hormone was purified by gel filtration on Sephadex, resulting in a product that is soluble in water or 0.5% sodium chloride. It is painless on injection and shows a twofold increase in biological potency. Aggregation of growth hormone on Sephadex columns can...
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Electrophoresis is widely used as a separative technique, particularly in protein chemistry. In some respects gelatinous media have an advantage over others as support media for electrophoresis, perhaps most obviously when a gel matrix of molecular dimensions is employed, allowing the simultaneous use of two properties for separation of the particles of interest-size and surface charge density....
متن کاملTwo-dimensional Analysis of Skim Milk Proteins Using Preparative Isoelectric Focusing Followed by Polyacrylamide Gel Electrophoresis
A preparative isoelectric focusing (IEF) method was applied to separate skim milk proteins using the Rotofor device in a pH 3-10 gradient containing 4 M urealI % triton X-I 00. Each ofthe 20 fractions obtainedfrom the Rotofor device was then analyzed by polyacrylamide gel electrophoresis (PAGE). Both ureaPAGE and SDS-PAGE were used to separate purified caseins and skim milk resulting in compara...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1973
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.7.3.493-495.1973