Open AccessThree‐step procedure for preparation of pure Bacillus altitudinis ribonuclease
Author(s) -
Dudkina Elena,
Ulyanova Vera,
Shah Mahmud Raihan,
Khodzhaeva Vera,
Dao Linh,
Vershinina Valentina,
Kolpakov Alexei,
Ilinskaya Olga
Publication year - 2016
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1002/2211-5463.12023
Subject(s) - ribonuclease , chemistry , residue (chemistry) , alanine , amino acid , chromatography , biochemistry , cytotoxicity , threonine , amino acid residue , combinatorial chemistry , enzyme , serine , peptide sequence , rna , in vitro , gene
Ribonucleases are considered as promising tools for anticancer treatment due to their selective cytotoxicity against tumor cells. We investigated a new RN ase from Bacillus altitudinis termed BALNASE ( B . altitudinis RN ase). 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 RN ase might be changed by A106T substitution. Here, we have developed a chromatography‐based rapid and modern technique for the purification of this new RN ase 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.