22 February 2012
- Today, the proteins were isolated with a purification machine (GE AKTApurifier). The proteins were run through at 30% B solution (25mM Tris, 1M NaCl) in solution A (25 mM Tris, 50mM NaCl) to prevent the positively charged filter from attracting the negatively charged hemoglobin proteins. After being purified, they were put into containers and refrigerated.
- For February 15, the two solutions were mixed in the laboratory. Hemoglobin proteins without Heme were also sonicated to retroactively add Heme. This was done to three containers of hemoglobin. Each container was sonicated 2, 4, or 6 times, respectively.