MODIFIED HEMOGLOBINS AND THEIR REACTIONS WITH LIGANDS

除了与氧的相互作用外， 铁和亚铁氧化态与碳的氧化物相互作用， 氮和硫。 我们进行了一项试验性研究， 一种这样的配体，一氧化氮（NO）与许多 在杜克使用停流装置的化学修饰血红蛋白 大学海洋实验室，NC。 （NO）与 这些血红蛋白的铁形式显示出类似于 未经修饰的血红蛋白。 然而，初步分析显示， 修饰血红蛋白反应速率的明显差异 有（否）。 (NO)与修饰的血红蛋白的相互作用是 特别感兴趣的是，由于内皮衍生舒张因子（EDRF） 现在相信是（否）。 这些实验提供了一个框架， EDRF与各种药物相互作用的性质的体内研究 修饰的血红蛋白，可能会揭示一些关于血管收缩 血红蛋白溶液的活性。 最近，一个微体积停止流动 荧光分光光度计已安装在我们的实验室。 这是一个交钥匙 一种具有吸收、荧光和双重功能动力工作站 波长能力。 一个32位RISC处理器提供了一个完整的 数据采集和处理包沿着图形文件 屏幕管理系统 人们可以开始讨论如何 氧亲和力的变化影响配体的结合性质 交联血红蛋白与总氧平衡的关系 在组织中加载和卸载。 这可能最终直接影响到 肌红蛋白制剂的功效和毒性。

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.