PRIMARY AND SECONDARY BINDING SITES OF THE TRANSFERRINS

研究计划可分为五个部分。 1.血清转铁蛋白和乳转铁蛋白的次级金属结合部位。证据 来自氨基酸序列比对、EPR、动力学和分光光度 揭示了二次金属结合位点的存在。我想确定一下 它们的化学计量比，不同金属、金属的相对亲和力 交换反应性及其对初级金属/阴离子中心的影响。 2.乳转铁蛋白的铁交换活性。人们对此知之甚少 乳转铁蛋白攻击、隔离和释放的反应 铁制的。这一信息将有助于阐明可能的生理作用。 并提供了与以下数据的有价值的比较 血清转铁蛋白。3.环境和化学改性与铁 转铁蛋白的交换反应性。变性剂、pH、化学物质 改性、温度和盐分对位置有不同的影响 在转移者的两个肺叶中。我想知道修改后会发生什么变化 具有攻击性、封闭性和释铁性。有特殊利益的人 将深入了解导致构象变化的 铁和阴离子结合应力的稳定化。4.控制攻击， 阴离子结合部位对铁的截留和释放。《负离子》 结合部位控制蛋白质对铁和其他物质的亲和力 金属。这种现象可以通过使用碳酸盐来探索。 在研究金属离子侵蚀、隔离、氧化、 减少和释放。5.除铁以外的金属的交换 转铁蛋白。Transferrins提供了一个很好的模型系统 检测蛋白质对铜、锰、钴、铬、镍等金属离子的交换。我 我想发现管理金属离子交换的规则并学习 关于将金属引导到特定位置的机制。6.金属离子 转铁蛋白和其他蛋白质之间的交换。金属离子怎么样了？ 从一种蛋白质传递到另一种蛋白质？它是否总是通过调解人，如 螯合剂和氧化还原试剂？或通过修改力，例如 酸化？蛋白质-金属-蛋白质复合体形成吗？铜蓝蛋白， 磷高铁蛋白，血清、卵子和乳清转铁蛋白，血清白蛋白， 将以羧基肽酶A、铁蛋白为研究对象。7. 牛奶中的乳转铁蛋白和血清中的转铁蛋白。太少了 关注自然界中金属离子的交换反应。 环境。我希望将上面的许多工作扩展到生理学 感兴趣的媒体。

The Research Plan can be divided into five sections. 1. Secondary metal binding sites of sero- and lactotransferrin. Evidence from amino acid sequence comparisons, EPR, kinetics and spectrophotometry reveal the presence of secondary metal binding sites. I wish to ascertain their stoichiometry, relative affinities for different metals, metal exchange reactivities and their effect on the primary metal/anion sites. 2. Iron exchange reactivities of lactotransferrin. Little is known about the reactions in which lactotransferrin attacks, sequesters and releases iron. This information will shed light on possible physiological roles of lactotransferrin and provide a valuable comparison with the data on serotransferrin. 3. Environmental and chemical modification and the iron exchange reactivities of the transferrins. Denaturants, pH, chemical modification, temperature and salts have a differential effect on the sites in the transferrins' two lobes. I want to know how the modification alters the attack, sequestration and iron release properties. Of special interest will be insight into the conformational change that results in the labilization of the iron and anion binding stress. 4. Control of attack, sequestration and release of iron by the anion binding site. The anion binding site controls the affinity of the protein for iron and other metals. This phenomenon can be explored via the use of carbonate substitutes in studies of metal ion attack, sequestration, oxidation, reduction and release. 5. Exchange of metals other than iron by the transferrins. The transferrins offer an excellent model system for examining protein metal ion exchange for Cu, Mn, Co, Cr, Ni and others. I want to discover the rules that govern exchange of metal ions and to learn about the mechanisms that direct metals to specific sites. 6. Metal ion exchange between the transferrins and other proteins. How are metal ions passed from one protein to another? Is it always via mediators such as chelators and redox reagents? or via a modification force such as acidification? Do protein-metal-protein complexes form? Ceruloplasmin, phosvitin, the sero-, ovo- and lactotransferrins, serum albumin, carboxypeptidase A, ferritin will be subjects of study. 7. Lactotransferrin in milk and serotransferrin in serum. Too little attention is paid to the metal ion exchange reactivities in the natural environment. I wish to extend much of the work above to the physiological media of interest.