Replacement of asparagine by aspartic acid in hen ovalbumin and a difference in immunochemical reactivity.
Replacement of asparagine by aspartic acid in hen ovalbumin and a difference in immunochemical reactivity.
复制标题
母鸡卵清蛋白中天冬酰胺被天冬氨酸替代以及免疫化学反应性的差异。
作者：
R. Wiseman;J. Fothergill;L. Fothergill
通过物理和免疫化学技术对以遗传变异形式存在的两种形式的母鸡卵清蛋白进行了比较。这两种卵蛋白可以通过电泳迁移率和用异种抗原处理过的抗血清来区分。两种卵蛋白的胰凝乳蛋白酶酶切图谱显示，三种多肽是不同的。对这些细菌进行了分离和分析。一种形式的卵清蛋白(类型B)包含序列：-Ser-Ser-Ala-Asp-Leu-Ser-Gly-Ile-Ala-Glu-Ser(Ser，(亮氨酸)-，而另一种形式(类型A)包含天冬酰胺残基代替天冬氨酸残基。A型的-Asn-Leu-Ser-序列不是糖基化的。凝乳酶很容易在含有天冬酰胺的多肽中裂解亮氨酸-丝氨酸键，但在含有天冬氨酸的变异体中则不能。
Two forms of hen ovalbumin that exist as genetic variants were compared by physical and immunochemical techniques. The two ovalbumins could be distinguished by electrophoretic mobility and by antisera that had been pretreated with heterologous antigen. Peptide ;maps' of chymotrypsin digests of the two ovalbumins revealed that three of the peptides were different. These were isolated and analysed. One form of ovalbumin (type B) contains the sequence: -Ser-Ser-Ala-Asp-Leu-Ser-Gly-Ile-Ala-Glu-Ser(Ser,Leu)- whereas the other form (type A) contains an asparagine residue in place of the aspartic acid residue. The -Asn-Leu-Ser- sequence of type A is not glycosylated. Chymotrypsin readily cleaved the leucine-serine bond in the asparagine-containing peptide, but not in the aspartic acid-containing variant.