Podila G K, Flurkey W H
Biochem Biophys Res Commun. 1986 Dec 15;141(2):697-703. doi: 10.1016/s0006-291x(86)80228-5.
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.
蘑菇酪氨酸酶被纯化，并制备了针对全酶和一种26000道尔顿蛋白质的抗体。两种抗体都能识别该酶的大亚基，但只有一种能识别26000道尔顿的蛋白质。从蘑菇中分离出多聚腺苷酸加尾的信使核糖核酸（Poly A+ mRNA），在体外进行翻译，并用任何一种抗体从翻译混合物中免疫沉淀出一种41000道尔顿的蛋白质。这种41000道尔顿的蛋白质可能对应于全酶的大亚基。针对全酶的抗体还免疫沉淀出另一种分子量为15000道尔顿的翻译产物，它对应于全酶的小亚基。这些结果表明，每个亚基可能由不同的基因编码，并经历翻译后加工。
