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    • The minor anionic form of arylsulphatase B (arylsulphatase Bm) of monkey brain. Purification and phosphoprotein nature

      S Lakshmi A S Balasubramanian

      Volume 6 Issue 1 March 1984 pp 79-85

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      Permanent link:
      https://www.ias.ac.in/article/fulltext/jbsc/006/01/0079-0085

    • Keywords

       

      Arylsulphatase Bm; monkey brain; purification; phosphoprotein

    • Abstract

       

      The anionic form of arylsulphatase B (arylsulphatase Bm) was purified to apparent homogeneity from monkey brain through steps involving chromatography on diethylaminoethyl-cellulose, Blue-Sepharose, Biogel HTP and finally Biogel P-300 gel filtration. The molecular weight of the purified enzyme as deduced by gel filtration on Biogel P-300 and by sodium dodecylsulphate gel electrophoresis was ∼ 30,000.Escherichia coli alkaline phosphatase treatment of arylsulphatase Bm resulted in the conversion of upto 84% of the enzyme into a less charged form of enzyme, that could not bind to diethylaminoethyl cellulose. Potassium phosphate an inhibitor of alkaline phosphatase prevented this conversion. Upon acid hydrolysis the purified enzyme yielded approximately 7.0 mol of inorganic phosphate per mol of protein.Vibrio cholerae neuraminidase treatment did not alter the charge on arylsulphatase Bm.

    • Author Affiliations

       

      S Lakshmi1 A S Balasubramanian1

      1. Neurochemistry Laboratory, Department of Neurological Sciences, Christian Medical College and Hospital, Vellore - 632 004, India

    • Dates

       
      Published
      March 1984
      Manuscript received
      26 August 1983

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