Author:
Arora D. J. S.,Hill-Schubert J.,Vincent L.
Abstract
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.
Publisher
Canadian Science Publishing
Subject
Genetics,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Immunology,Microbiology
Cited by
6 articles.
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