Increased Morbidity and Its Possible Link to Impaired Selenium Status

Abstract

This chapter summarizes the latest information on the main differences in the chemical properties of selenium proteins and their sulfur analogues, Se proteins and their functions, Se-accumulating proteins, the relationship between Se and hemoglobin, Selenium in gerontology, Selenium and iodine deficiency conditions, Se and immunity, Selenium as an antioxidant in nitrite poisoning. Also discussed are some of the results of the first studies on protein enrichment with selenium carried out in the seventies of the last century. This native protein was natural silk fibroin. Fibroin has since become an important tool for human health and healing. It was discovered that when selenium-containing inorganic compounds were added to mulberry silkworm feed, selenium atoms formed additional sulfur-like bonds in fibroin macromolecules. This resulted in additional branching of protein macromolecule. Selenium atoms in the fibroin structure have a sufficiently high electron affinity, act as small traps and capture migrating electrons. This leads to a reduction of free radicals, which are generated by external influences such as mechanical, thermal, electrical and radiation.