Arora D J, Hill-Schubert J, Vincent L
Can J Microbiol. 1980 Feb;26(2):243-9. doi: 10.1139/m80-037.
The wild type influenza strain A/Aichi/2/68 (H3N2), when disrupted with SDS and electrophoresed on cellulose acetate paper, yielded two separate neuraminidases, NA(H+) and NA(H-). These enzymes after extraction were biologically active and possessed different specific activities. Enzyme NA(H+) possessed neuraminidase as well as hemagglutinin activities whereas enzyme NA(H-) demonstrated only neuraminidase activity. Similar results were obtained when the Aichi strain was treated with Tween-ether and the two enzymes were separated by affinity chromatography. Techniques used failed to separate the hemagglutinin activity from neuraminidase NA(H+). These results suggest that the dual activity present in enzyme NA(H+) may be characteristic of this protein. Both enzymes are antigenically different and are apparently present as distinct entities in the Aichi strain. Experiments showed that only enzyme NA(H-) of the Aichi strain was incorporated into the hybrid X-32 virus during genetic recombination.
野生型甲型流感病毒株A/爱知/2/68（H3N2）经十二烷基硫酸钠处理并在醋酸纤维素纸上进行电泳后，产生了两种不同的神经氨酸酶，即NA(H+)和NA(H-)。提取后的这些酶具有生物活性，且具有不同的比活性。酶NA(H+)具有神经氨酸酶以及血凝素活性，而酶NA(H-)仅表现出神经氨酸酶活性。当用吐温 - 乙醚处理爱知株并通过亲和层析分离这两种酶时，也得到了类似的结果。所使用的技术未能将血凝素活性与神经氨酸酶NA(H+)分离。这些结果表明，酶NA(H+)中存在的双重活性可能是该蛋白质的特征。这两种酶在抗原性上不同，并且在爱知株中显然以不同的实体形式存在。实验表明，在基因重组过程中，爱知株中只有酶NA(H-)被整合到杂交X - 32病毒中。
