Hi, Why is there 2 different molecular masses of a denatured enzyme? The original enzyme has molecular mass of 266kDa, but after denatured with urea and mercaptoethanol, 2 different values were obtained, 105kDa and 150kDa. Thank you.
what do you mena it has 2 different values? did you seperate it and then measure both parts? I am not terribly well learned in enzymes but I will be willing to bet it is an outside force. Was this even an experiment you did? Does this belong on the biology forum? Am I asking to many questions? More information please.
Probably because the native enzyme is comprised of multiple subunits, like so many enzymes are. Under denaturing conditions the multimer disassociates into individual subunits (ie. individual proteins) and run separately. In this case it appears as though there are two subunits of 105kDa and 150kDa.
