We have developed a facile means for the refolding of milligram quantities of purified proteins that employs gel filtration chromatography. We demonstrate by electrophoretic mobility shift and NMR spectroscopy that human ETS-1 protein, bovine ribonuclease A and E. coli integration host factor can be refolded into the native conformation using this technique. We have extended this strategy to th...

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...

The elution pattern of serum proteins and the distribution of rubella HAI activity in 95 sera from 65 cases were determined after gel filtration with (a) Sephadex G-200 and (b) Bio-Gel A-5M. Rubella HAI antibody in peak 1 after Sephadex G-200 fractionation of early convalescent sera consists of both IgM and high molecular weight IgA. However, these two classes of antibody can be distinguished b...

A polysaccharide depolymerase was puritied 1,688-fold from crude lysates produced by the propagation of a specitic bacteriophage in Pseudomonas aeruginosa. Conventional methods of protein fractionation were employed, namely, salting out with ammonium sulfate, Sephadex gel filtration, and high speed centrifugation. The purified depolymerase behaves as a single entity when tested by electrophores...

A polysaccharide depolymerase was puritied 1,688-fold from crude lysates produced by the propagation of a specitic bacteriophage in Pseudomonas aeruginosa. Conventional methods of protein fractionation were employed, namely, salting out with ammonium sulfate, Sephadex gel filtration, and high speed centrifugation. The purified depolymerase behaves as a single entity when tested by electrophores...

The molecular weight of IgG3 myeloma proteins is about 170,000 as judged by gel filtration analyses of the light and heavy chains in 5 M guanidine-1 M acetic acid. The heavy chain of IgG3 has a molecular weight of about 60,000, which is larger by 9,000 to 10,000 than the molecular weight of the heavy chain of IgGl. Under nondenaturing conditions, an apparent molecular weight of 200,000 is obtai...