In vitro translation of mushroom tyrosinase.
Mushroom tyrosinase was purified and antibodies prepared against the holo enzyme and a protein of 26,000 daltons. Both antibodies recognized the large subunit of the enzyme but only one recognized the 26,000 dalton protein. Poly A+ mRNA was isolated from mushrooms, translated in vitro, and a 41,000 dalton protein immunoprecipitated from the translation mix with either antibody. This 41,000 dalton protein presumably corresponds to the large subunit of the holoenzyme. Antibodies against the holoenzyme also immunoprecipitated another translation product with a molecular weight of 15,000 daltons corresponding to the small subunit of the holoenzyme. These results suggest that each subunit may be coded for by different genes and undergo posttranslational processing.
D001487:Basidiomycota; D004156:Catechol Oxidase / Q000235:genetics*; D002474:Cell-Free System; D005779:Immunodiffusion; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000235:genetics* / Q000276:immunology; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D012333:RNA, Messenger / Q000235:genetics
D012333:RNA, Messenger; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase