TY - JOUR

T1 - Dve formy vnekletochnoĭ nizkomolekuliarnoĭ ribonukleazy Bacillus sp. BCF 247. Vydelenie i kharakteristika belka

AU - Dement'ev, A A

AU - Golyshin, P N

AU - Riabchenko, N F

AU - Pustobaev, V N

AU - Shliapnikov, S V

PY - 1993/8

Y1 - 1993/8

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Bacillus/enzymology

KW - Chromatography, High Pressure Liquid

KW - Electrophoresis, Polyacrylamide Gel

KW - Hydrolysis

KW - Isoenzymes/chemistry

KW - Mass Spectrometry

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Ribonucleases/chemistry

M3 - Erthygl

C2 - 8399775

VL - 58

SP - 1258

EP - 1265

JO - Biokhimiia (Moscow, Russia)

JF - Biokhimiia (Moscow, Russia)

SN - 0320-9725

IS - 8

ER -