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But if that second solution of glucose replaces the first one, wouldn't the protein come out bound with the second solution, thus making it still not clear?
I think the second solution should not be glucose, but some other molecule that has more affinity to the glucose attached to the bead, so that it will competitively bind to it making our protein/enzyme of interest free so that it moves down.
#Chromatography is the collective term for a set of laboratory techniques for the separation of mixtures. The separation is based on differential partitioning between the mobile and stationary phases. Commonly used chromatography techniques include: gel filtration, ion exchange chromatography, hydrophobic interaction chromatography and affinity chromatography. Creative BioMart contains all different types of chromatography at all scales of matrix include: cross-linked agarose, cross-linked cellulose, dextran, methacrylic and polystyrene.
this is a great video and I found it to be a helpful review for my studies. However as a friendly correction you stated that this technique is only useful "if you know what specific protein that molecule binds to" However, I believe you can use Affinity chromotography for undetermined binding. If you use s tag such as FLAG that is is very hydrophilic it can be used to bind / tag the protein to the column even if that have no known binding partner. Then you can look at similar family of proteins with known/potential binding partners and run those partners through the column to see what your proteins of interest binds to. This technique has been used in many publications such as " Optimal Translational Termination Requires C4 Lysyl Hydroxylation of Erf1" Feng Et AL. Again just a friendly correction. Thank you .
no such words could EVER show how thankful i am for you... my medical studies are in french and i don't get a word of what our prof say... but here you are explaining better than any prof could ever do!!! such a HERO
may I ask: 1. what can we do to ensure the enzyme will not digest, only binds with the immobilized substrate during running the column? 2. after step E, what methods can be used to extract the enzyme of interest i.e. separate them from the glucose solution and transfer them to a suitable buffer solution since there still exists a binding force?
Really you are amazing lecture i used to follow your lectures,but in this one i have a notes which is whats make free sugar solution pull glucose oxidase from its attracted state ?
avedesco You telling me green-blue colorblind tells me absolutely nothing. If you want me to correct something I might have said in this lecture, add an annotation to your comment so I can go straight to that point and make the appropriate corrections.
A great teacher ...really impressed by your way of teaching . Got to know about your lectures by random searching.Your dedication is reflecting in ur lectures ...
