New technique for rapid purification, entrapment, and recovery of enterotoxin A from a liquid chamber by polyacrylamide gel electrophoresis.

نویسندگان

  • P L Tan
  • C B Denny
  • W R Heilman
  • C W Bohrer
چکیده

Electrophoreis of enterotoxin into a middle liquid section of a polyacrylamide gel column enhances recovery for serological assay.

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

Improved method for purification of enterotoxin from Clostridium perfringens type A.

The purification procedure of Clostridium perfringens type A enterotoxin has been improved. The cell sonic extract was precipitated twice with ammonium sulfate, first 40% saturated to concentrate the enterotoxin and then 15% saturated. The two precipitations were followed by gel filtration on Sephadex G-100. The enterotoxin appeared to be homogeneous on 7% polyacrylamide gel electrophoresis aft...

متن کامل

Preparative polyacrylamide gel electrophoresis purification of Clostridium perfringens enterotoxin.

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...

متن کامل

Separation and isolation of fusion protein using a new native preparative PAGE device.

A human serum albumin and Thymosin α1 (HSA-Tα1) fusion protein was designed and over-expressed in Pichia pastoris. To purify the fusion protein, a new native preparative electrophoresis system that involved a modified device with a sample receiving chamber, and an assay method with Coomassie Blue G-250 tracing the collection of the protein of interest. In this device, two gels were run in paral...

متن کامل

Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.

Heat-labile enterotoxin (LT) was purified from an enterotoxigenic Escherichia coli 015H11 of human origin. The purification steps included French pressure cell disruption of the bacteria, salting-out, DEAE-Sephacel on chromatography. Application of this procedure resulted in a 95.1-fold purification of LT with a yield of 19.9% as determined by rabbit ileal loop assay. The final LT preparation s...

متن کامل

Rapid, simplified method for production and purification of tetanus toxin.

A rapid, simplified method for production and purification of tetanus toxin from bacterial extracts was described. The extracts were prepared by stirring young cells (ca. 45-h culture) of Clostridium tetani in 1 M NaCl-0.1 M sodium citrate, pH 7.5, overnight at 0 to 4 degrees C. The toxin was purified by a combination of (i) ammonium sulfate fractionation (0 to 40% saturation), (ii) ultracentri...

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:
  • Applied microbiology

دوره 18 6  شماره 

صفحات  -

تاریخ انتشار 1969