Статья

Three-step procedure for preparation of pure Bacillus altitudinis ribonuclease

E. Dudkina, V. Ulyanova, M. Shah, V. Khodzhaeva, L. Dao, V. Vershinina, A. Kolpakov, O. Ilinskaya,
2021

Ribonucleases are considered as promising tools for anticancer treatment due to their selective cytotoxicity against tumor cells. We investigated a new RNase from Bacillus altitudinis termed BALNASE (B. altitudinisRNase). Balnase is a close homolog of the well-known cytotoxic binase, differing by only one amino acid residue: nonpolar hydrophobic alanine at position 106 in the balnase molecule is replaced by a polar uncharged threonine in binase. The most exciting question is how the physico-chemical properties and biological effects of RNase might be changed by A106T substitution. Here, we have developed a chromatography-based rapid and modern technique for the purification of this new RNase which allowed us to get a protein sample of high quality with specific activity of 1.2 × 106units in preparative amounts, suitable for further investigation of its biological properties. © 2015 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.

Цитирование

Похожие публикации

Источник

Версии

  • 1. Version of Record от 2021-04-27

Метаданные

Об авторах
  • E. Dudkina
    Institute of Fundamental Medicine and Biology, Kazan Federal (Volga-Region) University, Russian Federation
  • V. Ulyanova
  • M. Shah
  • V. Khodzhaeva
  • L. Dao
  • V. Vershinina
  • A. Kolpakov
  • O. Ilinskaya
Название журнала
  • FEBS Open Bio
Том
  • 6
Выпуск
  • 1
Страницы
  • 24-32
Ключевые слова
  • alanine; balnase; ribonuclease; threonine; unclassified drug; Article; Bacillus; Bacillus altitudinis; bioinformatics; catalysis; enzyme activity; enzyme isolation; enzyme purification; hydrophobicity; immunoblotting; mass spectrometry; nonhuman; polyacrylamide gel electrophoresis; priority journal; zymography
Издатель
  • Elsevier B.V.
Тип документа
  • journal article
Тип лицензии Creative Commons
  • CC
Правовой статус документа
  • Свободная лицензия
Источник
  • scopus