Dve formy vnekletochnoĭ nizkomolekuliarnoĭ ribonukleazy Bacillus sp. BCF 247. Vydelenie i kharakteristika belka
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In: Biokhimiia (Moscow, Russia), Vol. 58, No. 8, 08.1993, p. 1258-65.
Research output: Contribution to journal › Article › peer-review
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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 -