[Primary structure and catalytic properties of extracellular ribonuclease from Bacillus circulans].
A comparative research of individual peptide structures obtained after hydrolysing of Bacillus circulans and B. amyloliquefaciens RNases by the Glu-specific staphylococcal protease was carried out by means of mass-spectrometry and Edman degradation methods. A complete amino acid sequence of B. circulans RNase was determined. Gln15, Gly65 and Gln104 residues in B. amyloliquefaciens RNase were found to be substituted by Leu, Ala and Lys residues in B. circulans RNase, respectively. Catalytic properties of the B. circulans RNase in transesterification reactions with poly- and oligonucleotides as substrates were investigated.
Dement'ev
A A
AA
Moiseev
G P
GP
Shliapnikov
S V
SV
D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D006868:Hydrolysis; D007700:Kinetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D012697:Serine Endopeptidases
D012260:Ribonucleases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase
Pervichnaia struktura i kataliticheskie svoĭstva vnekletochnoĭ ribonukleazy Bacillus circulans.