[Two forms of extracellular low molecular weight Bacillus sp. BCF 247 ribonuclease. Isolation and characteristics of the protein].
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.
Dement'ev
A A
AA
Golyshin
P N
PN
Riabchenko
N F
NF
Pustobaev
V N
VN
Shliapnikov
S V
SV
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D012260:Ribonucleases / Q000737:chemistry / Q000302:isolation & purification*
D007527:Isoenzymes; D012260:Ribonucleases