Separation And Structure Study Of F₁-ATP Synthase

This aritcal try to detected F₁-ATP syntheses with polyacrylamide gel electrophoresis which are extracted from different organizes.Considering the resemblance between paper chromatography and electrophoresis on distinguishing mixture of different monosaccharides or amino acids and eluting of interest component,we have a try to separate the components of some amylases which have been hydrolyzed by paper chromatography before polyacrylamide gel electrophoresis.Amylases in this experimentation are available.After the separation of monosaccharides,we found a better separation of Schisandra Chinensis polysaccharide AP4.It may be cause by its purity and much more components.Although the method of paper chromatography is good at some polysaccharide in this article,its resolution is lower in some degree.As to polyacrylamide gel electrophoresis,we used two different nondenaturing polyacrylamide gel electrophoresis.One is no dye during the electrophoresis,we called it colorless native-PAGE,ie.CN-PAGE.And the other one is named BN-PAGE for the existent of commassie blue G_-250.Differing from linear gradient gels,native-page in this article is of uniform concentration.And we gained some good outcome that F₁-ATP synthase could be separated from other proteins better.AFM is used after elution of F₁-ATP synthase from polyacrylamide gels. The AFM picture shows more than one kind of dimension.It means that there are two or three proteins.So,resolution of polyacrylamide gel electrophoresis with uniform concentration is not high enough to separate it from others.After polyacrylamide gel electrophoresis,proteins were eluted from the interest bands.Then, concentrate the solution of eluted protein by PEG.,and detected them by AFM.The result shows that these F₁-ATP synthase have a different size with it of former reports.It may be caused by the AFM probe or process of us.So,purification and observation of F₁-ATP synthase are to be improved.