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Title: Characterization of a soluble inorganic pyrophosphatase from Microcystis aeruginosa and preparation of its antibody
Authors: Kang, C.B.H.
Ho, K.K. 
Issue Date: 15-Aug-1991
Citation: Kang, C.B.H.,Ho, K.K. (1991-08-15). Characterization of a soluble inorganic pyrophosphatase from Microcystis aeruginosa and preparation of its antibody. Archives of Biochemistry and Biophysics 289 (1) : 281-288. ScholarBank@NUS Repository.
Abstract: A soluble inorganic pyrophosphatase was isolated from a crude extract of Microcystis aeruginosa by adsorption chromatography. The enzyme was purified to homogeneity as judged by sodium dodecyl sulfate (SDS) and non-denaturing polyacrylamide gel electrophoresis and N-terminal amino acid analysis. The molecular mass was estimated to be 80 kDa by gel filtration chromatography, 87 kDa by nondenaturing polyacrylamide gel electrophoresis, and 28 kDa by SDS-polyacrylamide gel electrophoresis. The enzyme has an isoelectric point of 4.5, which is similar to the pIvalues reported for other soluble inorganic pyrophosphatases. The sequence of 29 N-terminal amino acids was determined; only 4 of these amino acids are identical to those in the sequence of Saccharomyces cerevisiae inorganic pyrophosphatase. M. aeruginosa inorganic pyrophosphatase is a Mg2+-dependent enzyme exhibiting a pH optimum of around 7.5. Its Km value for inorganic pyrophosphate was estimated to be 1.30 mm. A specific antibody was raised in chicken to M. aeruginosa inorganic pyrophosphatase. No immunological cross-reactivity was seen when Western blots of partially purified S. cerevisiae or Escherichia coli inorganic pyrophosphatase were probed with the antibody. © 1991.
Source Title: Archives of Biochemistry and Biophysics
ISSN: 00039861
Appears in Collections:Staff Publications

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