BB-rel@ldeleger:BB-rel-9864452 JSONTXT

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bionlp-ost-19-BB-rel-train

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Id Subject Object Predicate Lexical cue
T1 0-89 Title denotes Isolation and properties of extracellular alkaline phosphatase from Bacillus intermedius.
T3 68-88 Microorganism denotes Bacillus intermedius
T2 90-956 Paragraph denotes Alkaline phosphatase (APase) was isolated from the culture liquid of the streptomycin-resistant strain of Bacillus intermedius S3-19 and purified as a homogeneous preparation by ion-exchange chromatography and FPLC. Electrophoresis and gel-filtration revealed that the active enzyme is a monomer with molecular weight of 46-47 kD. The enzyme possessed phosphomonoesterase and phosphodiesterase activities with maximal levels at pH 9.5 and 55 degreesC and was stable until 60 degreesC at pH 8.0-10.0. The isolated APase exhibits a broad specificity towards a wide variety of substrates. The effect of divalent metal ions and other reagents on its catalytic activities was studied. It was concluded that alkaline phosphatase of B. intermedius is similar to the secreted alkaline phosphatases from other Bacillus species in its physicochemical and catalytic properties.
T4 163-185 Phenotype denotes streptomycin-resistant
T5 196-222 Microorganism denotes Bacillus intermedius S3-19
T6 816-830 Microorganism denotes B. intermedius
T7 891-899 Microorganism denotes Bacillus
E1 196-222 Exhibits denotes Bacillus intermedius S3-19
R1 E1 T5 Microorganism Bacillus intermedius S3-19,Bacillus intermedius S3-19
R2 E1 T4 Property Bacillus intermedius S3-19,streptomycin-resistant