Date of Award
Bachelor of Science
Hemocyanin is a large molecular weight, oxygen carrying protein that is present in the hemolymph of mollusks and arthropods . Limulus, horseshoe crab, hemocyanin is made up of 48 hexamer subunits ( consisting of seven different repeating subunits) each of which have oxygen binding dinuclear copper active centers. Octopus hemocyanin is composed of a single kind of polypeptide chain that has seven functional units, or oxygen binding domains.
The goals of research conducted by Gregory Cole and Danielle Mercatante during the fall of 1996 and spring of 1997 were to gain a biochemical understanding of the structure of Limulus and octopus hemocyanin. Experiments performed included: 1. Copper analysis of the amount of copper ions remaining in the active sites of all seven subunits of Limulus hemocyanin post DTT reaction; 2. Determination of whether the pH of Limulus hemocyanin prior to DTT reaction or the pH of the redialysis buffer determines the amount of oxygen binding capacity recovered; 3. Determination of whether the structure of Limulus Subunit IV changes over time; 4. Determination of whether EDTA affects the rate of the DTT reaction, oxygen binding capacity recovery, and the banding of the protein as seen by gel electrophoresis; and 5. Determination of the extent of stability the S-S bonds have on the copper active center in octopus hemocyanin, as seen by DTT reactions, copper analysis, and recovery of oxygen binding capacity post DTT reactions.
Mercatante, Danielle, "The stabilizing efects of disulfide bonds on Limulus and Octopus hemocyanin" (1997). Honors Theses. 1366.