INVESTIGATION OF FLAVIN SYSTEMS

继续调查将更全面地确定运输情况， 黄素的代谢和功能，尤其是涉及系统必需的 对包括人类在内的哺乳动物来说。特定的目的和信息的性质 研究内容包括：1.核黄素结合蛋白--比较性质 从不同的动物组织，发育方面，可能的手段 作为载体、荷尔蒙控制和详细分子的释放和功能 特点。2.黄酮症--包括自然界在内的分子性质 活性部位，底物诱导的性质，激素调节，以及 核黄素结合蛋白之间潜在的相互作用 底物和FAD合成酶，随后作用于产物。3. FAD合成酶--完全纯化，测定通用分子 属性，更详细地限定了衬底的具体特性，详细说明了 活动场所的性质，并评估监管控制和相互作用。 4.“共价”香料的生物合成和代谢--相对速率 颗粒所含黄素蛋白在体内的形成和周转， 也就是。线粒体定位的四个方面(如琥珀酸脱氢酶 和单胺氧化酶)和微粒体L-古龙内酯氧化酶，以及 氨基分解代谢的后续酶步骤 酸黄素亚组分。5.吡哆胺(吡哆醇)5‘-磷酸氧化酶 -黄素酶、底物、 产物和抑制剂，确定氢的立体专一性 催化提取、测序两条多肽链 活性单体，确定体内对FMN限速供应的依赖性 以及与核黄素状态相关的活性水平的定量。

Continuing investigations will determine more completely the transport, metabolism and function of flavins, especially as involve systems essential to mammals including humans. Specific aims and the nature of informatin sought include: 1. Riboflavin-binding proteins - comparative properties from different animal tissues, developmental aspects, probable means for release and function as carriers, hormonal control, and detailed molecular characteristics. 2. Flavokinase - molecular properties including nature of the active site, nature of substrate induction, hormonal regulation, and potential interactions between riboflavin-binding proteins that supply substrate and FAD synthetase which subsequently acts upon the product. 3. FAD synthesase - complete purification, determine general molecular properties, more throughly circumscribe substrate specificty, detail the nature of the active site, and assess regulatory control and interactions. 4. Biosyntheses and metabolism of "covalent" flavings - relative rates of formationa nd turnover in vivo of the particulately included flavoprotein, viz. the four of mitochondrial localization (e.g. succinate dehydrogenase and monoamine oxidase), and the microsomal L-gulonolactone oxidase, and subsequent enzymatic steps in the catabolic degradation of the amino acid-flavin subportions. 5. Pyridoxamine(pyridoxine)5'-phosphate oxidase - detail kinetics on binding and release of flavoenzyme, substrates, product and inhibitors, ascertain stereospecificity for hydrogen abstraction, sequence the two polypeptide chains of the catalytically active monomer, ascertain in vivo dependency on rate-limiting supply of FMN as well as quantitate level of activity as relates to riboflavin status.