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Three-step procedure for preparation of pure Bacillus altitudinis ribonuclease.


ABSTRACT: 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. altitudinis RNase). 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 × 10(6) units in preparative amounts, suitable for further investigation of its biological properties.

SUBMITTER: Dudkina E 

PROVIDER: S-EPMC4794795 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature

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Three-step procedure for preparation of pure Bacillus altitudinis ribonuclease.

Dudkina Elena E   Ulyanova Vera V   Shah Mahmud Raihan R   Khodzhaeva Vera V   Dao Linh L   Vershinina Valentina V   Kolpakov Alexei A   Ilinskaya Olga O  

FEBS open bio 20160119 1


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. altitudinis RNase). 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-che  ...[more]

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