MODIFIED HEMOGLOBINS AND THEIR REACTIONS WITH LIGANDS

除了它与氧气的相互作用外，它的两个体内的血红蛋白 铁和亚铁的氧化态与碳的氧化物相互作用， 氮气和硫磺。我们进行了一项试点研究，在这项研究中 一种这样的配体，一氧化氮(NO)与许多 杜克大学使用停流装置对血红蛋白进行化学修饰 北卡罗来纳州，大学海洋实验室。(NO)与(NO)的快速混合实验 铁形态的这些血红蛋白表现出类似于 未经修饰的血红蛋白。然而，初步分析显示， 修饰后的血红蛋白的反应速度有显著差异 有(否)。(否)与修饰的血红蛋白的相互作用是 特别感兴趣的是内皮源性松弛因子(EDRF) 现在被认为是(不)。这些实验提供了一个框架， EDRF与多种细胞因子相互作用性质的体内研究 修饰的血红蛋白可能会对血管收缩有所帮助 血红蛋白溶液的活性。最近，一个微小的体积停止了流动 我们实验室已经安装了荧光分光光度计。这是一把交钥匙 具有吸收、荧光和双重功能的动态工作站 波长能力。32位RISC处理器提供完整的 数据采集和处理包以及基于图形的文件 屏幕管理系统。人们可以开始解决这样一个问题：如何 氧亲和力的变化影响配体的结合性质 交联型血红蛋白与氧的总体平衡 在组织中装载和卸载。这最终可能会直接影响到 血红蛋白制剂的疗效和毒性。

In addition to its interaction with oxygen, hemoglobin in both its ferric and ferrous oxidation states interacts with oxides of carbon, nitrogen and sulfur. We carried out a pilot study in which the interaction of one such ligand, Nitric oxide (NO) with a number of chemically modified hemoglobins using the stopped flow apparatus at Duke University Marine Laboratory, NC. Rapid mixing experiments of (NO) with ferric forms of these hemoglobins show a biphasic kinetics similar to that of unmodified hemoglobin. However, initial analysis showed an appreciable difference in the rate of reactions of modified hemoglobins with (NO). (NO) interactions with modified hemoglobins are of particular interest since the endothelial derived relaxing factor (EDRF) is now believed to be (NO). These experiments provide a framework for in vivo studies on the nature of the interactions of EDRF with various modified hemoglobins that may shed some light on the vasoconstrictive activity of hemoglobin solutions. Recently, a microvolume stopped flow spectrofluorimeter has been installed in our lab. It is a turn key kinetic work station that features absorption, fluorescence and dual wavelength capabilities. A 32 bit RISC processor provides a complete data acquisition and processing package along with a graphics based file screen management system. One can begin to address the question of how changes in oxygen affinity affect ligands binding properties of crosslinked hemoglobins in relation to the overall balance of oxygen loading and unloading in tissue. This may ultimately bear directly on the efficacy and toxicity of the memoglobin preparations.