MECHANISMS OF HEMOGLOBIN POLYMERIZATION AND RED CELL AGGREGATION IN GOOSEFISH

本研究从两个方面对红鱼红细胞进行了研究：（1）α-SH （2）铜Ⅱ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，在体外聚合， 二硫键形成（Borgese等1988），鹅血红蛋白将 似乎易受细胞内氧化、聚合和 降低携氧能力。除了热不稳定性 （Borgese et all 1981），其高的自动氧化速率和 在氧化时聚合，关于功能知之甚少，并且 这种血红蛋白的结构或其可能的作用， 氧中毒 本调查将通过测量 (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）确定氨基酸组成和主要成分， Goosefish血红蛋白的序列。 在Cu==的浓度下， 对其他海洋硬骨鱼、板鳃类或 在无脊椎动物中，鹅血红蛋白是不可逆的聚集。 初步观察表明，一种机制可能是 通过外部取向膜的S-S键的异常交联 蛋白质，将继续。

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.