Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/5901
Title: Isolation and characterization of alkaline phosphatase of <i style="">Saccharopolyspora erythraea</i> from fermentation broth of erythromycin production
Authors: Bhattacharjee, Subhasree
Das, Ananta K
Mandal, Sunil K
Keywords: alkaline phosphatase
glycoprotein
native gel electrophoresis
PAS-staining
SDS-PAGE
<i style="">Saccharopolyspora erythraea</i>
Issue Date: Oct-2004
Publisher: CSIR
Series/Report no.: Int. Cl.<sup>7</sup> A 01 N 63/04
Abstract: Alkaline phosphatase having two <i style="">p</i>H optima (8.4 and 9.2) was excreted in substantial amount by <i style="">Saccharopolyspora</i> <i style="">erythraea</i> during erythromycin production and was precipitated from the broth with 60 - 80 % final saturation of ammonium sulphate. PAS and silver nitrate staining of SDS-gel electrophoresis depicted eight distinct bands of glycoproteins in the precipitate. Buffer A (<i style="">p</i>H 8.4) eluted the glycoproteins from native gels and showed four bands of phosphatase with optimum activity at <i style="">p</i>H 8.4 and four at <i style="">p</i>H 9.2. After three successive native gel electrophoreses and elutions, four isomers of <i style="">p</i>H 8.4 were isolated with Buffer A and four of <i style="">p</i>H 9.2 with Buffer B (<i style="">p</i>H 9.2). The eight isoenzymes of alkaline phosphatase were purified more than 20-folds and were characterized as glycoproteins of different molecular weights, turnover numbers and extensive sugar percentages in their molecules.
Description: 558-562
URI: http://hdl.handle.net/123456789/5901
ISSN: 0975-0967 (Online); 0972-5849 (Print)
Appears in Collections:IJBT Vol.03(4) [October 2004]

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