欧洲螈中的多种血红蛋白：它们被巯基化合物降解的情况

Multiple hemoglobins in Triturus cristatus: their degradation by sulfhydryl compounds.

Grasso J A, Casale G P, Chromey N C

Department of Anatomy, University of Connecticut Health Center, Farmington 06032.

Comp Biochem Physiol B. 1979;63(1):93-101. doi: 10.1016/0305-0491(79)90240-2.

Abstract

Hemolysates of newt (Triturus cristatus) red cells contain four distinct hemoglobin species which have been observed consistently both in individual animals and pooled samples. 2. Hemoglobin heterogeneity in the species arises from existence of multiple hemoglobulins, with no indication of genetic polymorphism. 3. While the relative proportions of the different hemoglobins may vary in different samples, HbII is usually the most abundant, with HbIII and HbIV constituting most of the remainder of the total hemoglobin complement. HbI never exceeds 3-5% of the total hemoglobin. 4. Neither the electrophoretic migration nor the anion exchange properties of the four hemoglobin species are altered by conversion of oxyhemoglobin to the cyanmet derivative, excluding artifacts due to different oxidation states of iron. 5. The average molecular weight of newt total hemoglobulin is 67,182 with no indication of hemoglobin polymers. 6. The use of sulfhydryl-reducing agents (mercaptoethanol, dithiothreitol) as a precaution against aggregation results in extensive degradation of newt hemoglobin through a process similar to "coupled oxidation" by ascorbate. 7. The degradative effects of sulfhydryl-reducing agents on newt hemoglobin suggest that these reagents be used cautiously in any hemoglobin analysis.

摘要

蝾螈（Triturus cristatus）红细胞的溶血产物含有四种不同的血红蛋白，在个体动物和混合样本中均持续观察到。2. 该物种中的血红蛋白异质性源于多种血红蛋白的存在，未显示出遗传多态性。3. 虽然不同样本中不同血红蛋白的相对比例可能有所不同，但HbII通常最为丰富，HbIII和HbIV构成了总血红蛋白其余部分的大部分。HbI从未超过总血红蛋白的3 - 5%。4. 将氧合血红蛋白转化为氰化高铁衍生物后，四种血红蛋白的电泳迁移率和阴离子交换特性均未改变，排除了由于铁的不同氧化态导致的假象。5. 蝾螈总血红蛋白的平均分子量为67,182，未显示出血红蛋白聚合物的迹象。6. 使用巯基还原剂（巯基乙醇、二硫苏糖醇）作为防止聚集的预防措施，会通过类似于抗坏血酸“偶联氧化”的过程导致蝾螈血红蛋白大量降解。7. 巯基还原剂对蝾螈血红蛋白的降解作用表明，在任何血红蛋白分析中都应谨慎使用这些试剂。