When.com Web Search

Search results

  1. Results From The WOW.Com Content Network
  2. Gel electrophoresis of proteins - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis_of...

    Proteins separated by SDS-PAGE, Coomassie brilliant blue staining. Protein electrophoresis is a method for analysing the proteins in a fluid or an extract. The electrophoresis may be performed with a small volume of sample in a number of alternative ways with or without a supporting medium, namely agarose or polyacrylamide.

  3. Zymography - Wikipedia

    en.wikipedia.org/wiki/Zymography

    A common protocol used in the past for zymography of α-amylase activity was the so-called starch film protocol of W.W. Doane. Here a native PAGE gel was run to separate the proteins in a homogenate. Subsequently, a thin gel with starch dissolved (or more properly, suspended) in it was overlaid for a period of time on top of the original gel. [6]

  4. Gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Gel_electrophoresis

    A specific experiment example of an application of native gel electrophoresis is to check for enzymatic activity to verify the presence of the enzyme in the sample during protein purification. For example, for the protein alkaline phosphatase, the staining solution is a mixture of 4-chloro-2-2methylbenzenediazonium salt with 3-phospho-2 ...

  5. QPNC-PAGE - Wikipedia

    en.wikipedia.org/wiki/QPNC-PAGE

    QPNC-PAGE, or Quantitative Preparative Native Continuous Polyacrylamide Gel Electrophoresis, is a bioanalytical, one-dimensional, high-resolution and high-precision electrophoresis technique applied in biochemistry and bioinorganic chemistry to separate proteins by isoelectric point and by continuous elution from a gel column for further characterization.

  6. Eastern blot - Wikipedia

    en.wikipedia.org/wiki/Eastern_blot

    (1982) The term eastern blotting was specifically rejected by two separate groups: Reinhart and Malamud referred to a protein blot of a native gel as a native blot; [3] Peferoen et al., opted to refer to their method of drawing sodium dodecyl sulfate-gel separated proteins onto nitrocellulose using a vacuum as Vacuum blotting. [4] [5]

  7. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    Isoelectric focusing is the first step in two-dimensional gel electrophoresis, in which proteins are first separated by their pI value and then further separated by molecular weight through SDS-PAGE. Isoelectric focusing, on the other hand, is the only step in preparative native PAGE at constant pH. [5]

  8. AOL Mail

    mail.aol.com

    Get AOL Mail for FREE! Manage your email like never before with travel, photo & document views. Personalize your inbox with themes & tabs. You've Got Mail!

  9. Two-dimensional gel electrophoresis - Wikipedia

    en.wikipedia.org/wiki/Two-dimensional_gel...

    Two-dimensional gel electrophoresis, abbreviated as 2-DE or 2-D electrophoresis, is a form of gel electrophoresis commonly used to analyze proteins. Mixtures of proteins are separated by two properties in two dimensions on 2D gels. 2-DE was first independently introduced by O'Farrell [ 1 ] and Klose [ 2 ] in 1975.