Two homogeneous samples of low molecular mass RNAase (RNAases Bci I and Bci II) were obtained from cultural filtrates of spore-forming bacteria strain Bacillus sp. BCF 247 isolated from permafrost soils. The yields of RNAases Bci I and Bci II were 17% and 16% at the 17388- and 15376-fold degree of purification, respectively. Both enzymes have a close specific activity which is equal to approximately 4.7 x 10(-5) activity units per mg of protein. The relative molecular masses of the isolated proteins were determined and their N-terminal amino acid sequences identified. It was shown that the higher molecular mass sample of the enzyme is a pro-RNAase which, in contrast with the mature protein, contains an additional decapeptide segment in the N-terminal part of its molecule. The structure of RNAase Bci was compared with that of RNAases obtained from other Bacillus species; its ability to interact with a natural intracellular inhibitor of B. amyloliquefaciens RNAase was demonstrated.

Keywords

  • Amino Acid Sequence, Bacillus/enzymology, Chromatography, High Pressure Liquid, Electrophoresis, Polyacrylamide Gel, Hydrolysis, Isoenzymes/chemistry, Mass Spectrometry, Molecular Sequence Data, Molecular Weight, Ribonucleases/chemistry
Original languageRussian
Pages (from-to)1258-65
Number of pages8
JournalBiokhimiia (Moscow, Russia)
Volume58
Issue number8
Publication statusPublished - Aug 1993
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