How do I separate the proteins that make up the triple helix? Nor can I measure proteins by Bradford for the same solubility problem. I appreciate suggestions
what is the approximate concentration of the collagen solution you obtained? What is the pH of the solution, did you measured it? Above 5 g/l the solutions get very viscous, nearly gel-like (although it is not a gel since you need to increase pH and inonic strength to get allow physical crosslinking).
I suggest you take a small amount and try to dilute with acetic acid 0.01 M.
I think it would better that you take a small amount and try to dilute with 8 M Urea, afterwrd,Concentration is achieved by spectrophotometer,and then It will be good to run the various concentrations of your protein to have control over reproducibility of the process.
Hi, thanks for your answers. The sample actually comes from bovine tendon. Not pig skin. I try to dissolve it in urea 9M, in acetic 0.5 M, in SDS 0.5% but it remains insoluble. I think it will be impossible to measure proteins or run a gel in these condition