PATHOPHYSIOLOGY OF ZINC

Autor: Milos Chvapil, Charles F. Zukoski, Sharon L. Elias, Janet N. Ryan
Rok vydání: 1972
Předmět:
DOI: 10.1016/b978-0-12-366851-6.50010-7
Popis: Publisher Summary This chapter discusses the pathophysiology of zinc. The stability of various biological macromolecules is dependent on or increased by the presence of zinc. Zinc is involved in the polymerization process, and it is the zinc-insulin complex that is stored in granules. Zinc also binds to DNA nucleoside bases and can be used in vitro to reversibly wind and unwind DNA double helices with heating and cooling. Zinc binds quite weakly to complementary bases so that when the DNA is cooled, the double helix can form again in both directions from the crosslink. Zinc ions bind strongly enough to phosphate to stabilize the double helix at lower temperatures. Zinc inhibits electron transport in the mitochondrial respiratory chain at very low concentrations, which suggests a rather effective and specific role of this metal in the control of respiration even in vivo. The membrane of cells and subcellular particles contain lipoprotein glycosaminoglycan macromolecules, which are either integral parts of this structure or are closely associated with the membrane.
Databáze: OpenAIRE