Sobocinski P Z, Canterbury W J, Mapes C A, Dinterman R E
Am J Physiol. 1978 Apr;234(4):E399-406. doi: 10.1152/ajpendo.1978.234.4.E399.
Hypozincemia was induced in rats by Salmonella typhimurium and live vaccine strain Francisella tularensis (LVS) infections. Hepatic synthesis of zinc-binding proteins (ZBP) was studied in order to elucidate the mechanisms involved in the redistribution of zinc from plasma to liver occurring during infectious illness. ZBP, labeled in vivo with 65Zn, were isolated and identified as metallothioneins based, in part, on their heat stability, dimorphism, and amino acid composition. Cysteine was the major amino acid found in both forms of metallothionein and constituted 28-31% of total residues. The apparent half-life of these proteins as measured by disappearance of 65Zn was determined to be 19 h in a relatively mild infection (LVS) and 38 h in a more severe S. typhimurium infection. Results provide evidence that metallothioneins not only have the previously postulated regulatory role in normal zinc homeostasis but are intimately involved in the zinc redistribution occurring during the acute stage of infectious illness.
通过鼠伤寒沙门氏菌和土拉弗朗西斯菌（LVS）活疫苗株感染诱导大鼠出现低锌血症。研究肝脏中锌结合蛋白（ZBP）的合成，以阐明在感染性疾病期间锌从血浆重新分布到肝脏所涉及的机制。体内用65Zn标记的ZBP被分离出来，部分基于它们的热稳定性、二态性和氨基酸组成，被鉴定为金属硫蛋白。半胱氨酸是在两种形式的金属硫蛋白中发现的主要氨基酸，占总残基的28 - 31%。在相对轻度的感染（LVS）中，通过65Zn的消失测定这些蛋白质的表观半衰期为19小时，在更严重的鼠伤寒沙门氏菌感染中为38小时。结果提供了证据，表明金属硫蛋白不仅在正常锌稳态中具有先前假设的调节作用，而且密切参与感染性疾病急性期发生的锌重新分布。
