title: Primary structure and catalytic properties of extracellular ribonuclease of Bacillus circulans.
abstract: A complete amino acid sequence of extracellular Bacillus circulans RNase was established and compared with a structure of B. amyloliquefaciens RNase. Gln15, Gly65 and Gln104 in B. amyloliquefaciens RNase were found to be replaced by Leu, Ala and Lys, respectively, in B. circulans RNase. Catalytic properties of B. circulans RNase were studied.
authors.affiliation: Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow.
authors.forename: A A
authors.initials: AA
authors.lastname: Dementiev
authors.forename: G P
authors.initials: GP
authors.lastname: Moiseyev
authors.forename: S V
authors.initials: SV
authors.lastname: Shlyapnikov
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D007700:Kinetics; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D010446:Peptide Fragments; D012260:Ribonucleases; C084264:ribonuclease Bci