Properties of retroviral protease responsible for gag precursor cleavage.
Friend Leukemia Virus (FLV) particles contain a protease which cleaves not only its own gag precursor but also the gag polyprotein of simian sarcoma virus (SSV). To determine the localization of the enzyme within the virion, purified virus was fractionated. According to our studies most of the proteolytic activity is located within the retroviral core. Since ionic detergents inhibit the protease, heat treatment was found to be the most effective way to release the molecule from the virus particle. The in vitro studies indicate a high resistance of the enzyme to different kinds of heat treatment.
Hafenrichter
R
R
Federal Research Centre for Virus Diseases of Animals, Tübingen, Federal Republic of Germany.
Weiland
F
F
Schneider
J
J
Thiel
H J
HJ
D002451:Cell Compartmentation / Q000187:drug effects; D003902:Detergents / Q000494:pharmacology; D005622:Friend murine leukemia virus / Q000201:enzymology*; D015683:Gene Products, gag; D046911:Macromolecular Substances; D008970:Molecular Weight; D010447:Peptide Hydrolases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D012191:Retroviridae Proteins / Q000235:genetics*; D013696:Temperature; D014764:Viral Proteins / Q000648:ultrastructure
D003902:Detergents; D015683:Gene Products, gag; D046911:Macromolecular Substances; D012191:Retroviridae Proteins; D014764:Viral Proteins; D010447:Peptide Hydrolases