title: Specific alteration of Sendai virus glycoprotein subunits.
abstract: The alteration produced by chemical and physical agents in the structure and neuraminidase activity of Sendai virus glycoproteins was studied. While dissociation of glycoproteins with 1% sodium dodecyl sulphate (SDS), 2% beta-mercaptoethanol and 5 M urea for 2 min at 100 degrees C yielded the known HN and F subunits (mol. wts. 60,000 and 53,000), in the presence of 1% SDS the glycoproteins were converted into components with approximate mol. wts. of 60,000, 120, 000 and higher. Treatment of the glycoproteins with 2% beta-mercaptoethanol and 0.1% SDS favoured the formation of a single component with a mol. wt. of 75,000. The alterations in the glycoprotein structure were very likely caused by their free -SH groups content. An average value of 6 free -SH groups per glycoprotein subunit was estimated. Glycoproteins stored at 4 degrees C contained only 53,000 mol. wt. subunits. During storage a kind of conversion of 67,000 to 53,000 mol. wt. components took place, preserving about 60% of the initial neuraminidase activity.
mesh_terms: D006023:Glycoproteins / Q000378:metabolism*; D008623:Mercaptoethanol / Q000494:pharmacology*; D008970:Molecular Weight; D009439:Neuraminidase / Q000378:metabolism; D010222:Parainfluenza Virus 1, Human / Q000187:drug effects* / Q000378:metabolism; D011489:Protein Denaturation; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D013696:Temperature; D014357:Trypsin / Q000494:pharmacology*; D014764:Viral Proteins / Q000378:metabolism*
chemical_list: D006023:Glycoproteins; D014764:Viral Proteins; D012967:Sodium Dodecyl Sulfate; D008623:Mercaptoethanol; D009439:Neuraminidase; D014357:Trypsin