ロード中...
An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.
Utilizing a procedure for the purification of RNase P from Xenopus laevis germinal vesicle (GV) extracts, according to which the contamination by a large, cytoplasmic, cylindrical structure (1) is avoided, we demonstrate that the X.laevis enzyme, like the HeLa RNase P, is precipitated by anti-Th ant...
保存先:
| 主要な著者: | , , , |
|---|---|
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
1991
|
| オンライン･アクセス: | https://ncbi.nlm.nih.gov/pmc/articles/PMC329436/ https://ncbi.nlm.nih.gov/pubmed/1710353 |
| タグ: |
タグ追加
タグなし, このレコードへの初めてのタグを付けませんか!
|