[Varying stability of the disulfide bond linking the heavy and light polypeptides subunits of influenza A virus hemagglutinin].
Two-dimensional electrophoresis of influenza virus proteins in polyacrylamide gel under nonreducing (1st direction) and reducing (2nd direction) conditions showed some hemagglutinin polypeptides to lack the disulphide bond linking the heavy and light subunits. According to the results obtained, various influenza virus strains may be differentiated by the criterion of stability of disulphide polypeptides of hemagglutinin.
D000818:Animals; D001345:Autoradiography; D002642:Chick Embryo; D004220:Disulfides / Q000032:analysis*; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D006389:Hemagglutinins, Viral / Q000032:analysis* / Q000145:classification; D009980:Influenza A virus / Q000032:analysis*; D010455:Peptides / Q000032:analysis* / Q000145:classification
D004220:Disulfides; D006389:Hemagglutinins, Viral; D010455:Peptides
Razlichnaia stabil'nost' disul'fidnoĭ sviazi, skrepliaiushcheĭ tiazheluiu i legkiiu sub"edinitsy polipeptidov genaggliutinina virusov grippa A.