title: Association of a ribonuclease with the purified influenza virus.
abstract: Purified influenza virus contains ribonuclease activity. The enzyme does not hydrolyze viral RNA but both 28 S and 18 S host cell RNA are degraded forming large (about 16 S) and small (about 5 S) fragments with the release of the acid-soluble material. It has an optimum temperature of 37 degrees C, requires no divalent ions, and is inhibited by 0.1 M EDTA and 1% SDS. Treatment with 4 M urea increases enzymatic activity considerably (42%) but is not a prerequisite for eliciting ribonuclease activity suggesting that the enzyme is probably located near the surface of the virus particle. Results show that the observed enzyme activity is virus-associated as no host cell protein is detectable in the purified virus.
mesh_terms: D002474:Cell-Free System; D046508:Culture Techniques; D004492:Edetic Acid / Q000494:pharmacology; D006868:Hydrolysis; D011119:Polynucleotides / Q000378:metabolism; D012313:RNA / Q000378:metabolism; D012260:Ribonucleases / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology; D013696:Temperature; D014508:Urea / Q000494:pharmacology
chemical_list: D011119:Polynucleotides; D012967:Sodium Dodecyl Sulfate; D012313:RNA; D014508:Urea; D004492:Edetic Acid; D012260:Ribonucleases