磺胺偶氮-触珠蛋白的性质。

W Dobryszycka, T Guszczyński
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引用次数: 1

摘要

1. 用重氮磺胺酸对人接触珠蛋白中组氨酸残基的酪氨酸和两个结构异构体进行修饰。通过增加试剂/蛋白质摩尔比得到的触珠蛋白磺胺偶氮衍生物与血红蛋白络合后,过氧化物酶活性逐渐降低。2. 与10个单(磺胺偶氮)酪氨酸和2个单(磺胺偶氮)组氨酸形成的触珠蛋白衍生物导致6个抗原决定因子中的1个受阻,而与14个偶氮酪氨酸,1个C-4和2个C-2偶氮组氨酸的衍生物的免疫反应性降低了一半。3.从接触珠蛋白的低聚糖链中去除唾液酸使重氮磺胺酸更容易接近分子。4. 酪氨酸和组氨酸残基的磺胺偶氮修饰对接触珠蛋白与植物凝集素刀豆蛋白A的反应几乎没有影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Properties of sulfanilazo-haptoglobin.

1. Tyrosine and two structural isomers of histidine residues in human haptoglobin were modified with diazotized sulfanilic acid. Sulfanilazo-derivatives of haptoglobin obtained by increasing the reagent/protein molar ration showed gradual decrease of peroxidase activity when complexed with hemoglobin. 2. Formation of haptoglobin derivatives with ten mono(sulfanilazo)-tyrosines and two mono (sulfanilazo)histidines resulted in the blockage of one out of six antigenic determinants, whereas immunoreactivity of the derivative with fourteen azotyrosines, one C-4, and two C-2 azohistidines was decreased by half. 3. Removal of sialic acid from oligosaccharide chains of haptoglobin made the molecule more accessible to diazotized sulfanilic acid. 4. Sulfanilazo-modification of tyrosine and histidine residues was practically of no effect in the reaction of haptoglobin with plant lectin, concanavalin A.

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