Date of Award
9-1982
Document Type
Thesis
Degree Name
Master of Science
Department
Chemistry
Abstract
strong evidence suggests that the serum ferroxidases (ceruloplasmin andferroxidase II) promote the formation of Fe-III transferrin and thereby stimulate the turnover of iron from tissue stores. Ceruloplasmin is the major ferroxidase in human serum; whereas, ferroxidase II accotmts for an increased proportion of the activity in less highly developed animals. A large fold increase in total ferroxidase II activity was observed when both human and rabbit sera were subjected to gel-filtration on sephadex G-200. This indicated that whole serum might contain a potent inhibitor of ferroxidase II. Such an inhibitor has been isolated and purified to homogeneity by a combination of gel-filtration and ion exchange chromatography. It has a molecular weight of 64,0
Recommended Citation
Calisch, Melissa Page, "Isolation and characterization of the serum ferroxidase inhibitor" (1982). Master's Theses. 486.
https://scholarship.richmond.edu/masters-theses/486