MECHANISMS OF HEMOGLOBIN POLYMERIZATION AND RED CELL AGGREGATION IN GOOSEFISH

本研究从两个方面研究了鹅红细胞：(1)α-SH 血红蛋白和(2)铜诱导红细胞聚集。作为唯一的 据报道，海洋硬骨鱼有一种血红蛋白，它在体外通过 二硫键的形成(Borgese等人，1988)，鹅鱼血红蛋白会 似乎容易受到细胞内氧化、聚合和 携氧能力下降。除了它的热不稳定性 (Borgese Et All 1981)，它的高自氧化率和它的 氧化后的聚合，对其功能知之甚少。 这种血红蛋白的结构或其可能的保护作用 氧气中毒。这项调查将通过以下方式解决这些问题： (1)主要还原系统的活性和浓度 细胞(2)氧自由基清除剂的作用(3)因素 调节P50和(4)测定氨基酸组成和初级 鹅鱼血红蛋白的序列。在铜==浓度下，没有 对其他海洋硬骨鱼、棘鳃或其他海生硬骨鱼红细胞的影响 无脊椎动物、鹅类的血红蛋白不可逆转地聚集在一起。 初步观察表明，一种机制可能是 外向膜的S-S键的异常交联 蛋白质，将被追寻。

This study deals with two aspects of goosefish red cells: (1) a -SH hemoglobin and (2) Copper II induced red cell aggregation. As the only marine teleost reported to have a hemoglobin that polymerizes, in vitro, by disulfide bond formation (Borgese et al 1988), goosefish hemoglobin would appear to be vulnerable to intracellular oxidation, polymerization and a reduced oxygen carrying capacity. Aside from its thermal instability (Borgese et all 1981), its high rate of auto-oxidation and its polymerization upon oxidation, little is known about the function, and structure of this hemoglobin or its possible role in protecting against oxygen toxicity. This investigation will address these issues by measuring (1) the activity and concentrations of the principal reducing systems of the cell (2) the effect of scavengers of oxygen radicals (3) factors regulating P50 and (4) determining the amino acid composition and primary sequence of goosefish hemoglobin. At concentrations of Cu== which have no effect on the red cells of other marine teleosts, elasmobranchs or invertebrates, goosefish hemoglobins are irreversibly aggregated. Preliminary observations, which suggest that one mechanism may be an unusual cross-linking by S-S bonds of externally oriented membrane proteins, will be pursued.