Please use this identifier to cite or link to this item:
|Title:||Characterization of a soluble inorganic pyrophosphatase from Microcystis aeruginosa and preparation of its antibody|
|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|
|Appears in Collections:||Staff Publications|
Show full item record
Files in This Item:
There are no files associated with this item.
checked on Oct 19, 2018
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.