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Soluble arylsulfatases of human brain and some characteristics of the brain-specific arylsulfatase Bm.

Authors
  • Lakshmi, S
  • Balasubramanian, A S
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Aug 07, 1980
Volume
614
Issue
2
Pages
446–458
Identifiers
PMID: 6105886
Source
Medline
License
Unknown

Abstract

The brain-specific arylsulfatase Bm (aryl-sulfate sulfohydrolase, EC 3.1.6.1) was demonstrable in human and monkey brain. Arylsulfatases A, B and Bm were separated employing DEAE-cellulose chromatography. There was a distinct difference in the proportion of the sulfatases in infant and adult human brain. Arylsulfatase Bm after concanavalin A-Sepharose chromatography showed the property of binding to Sephadex G-200 totally. Several dissociating agents failed to elute the enzyme from the bound form. Under similar conditions arylsulfatase A did not show any binding to Sephadex. On treatment with Escherichia coli alkaline phosphatase adult human brain arylsulfatase Bm but not arylsulfatase A was converted into a less acidic, presumably dephosphorylated form that did not bind to DEAE-cellulose. Monkey brain arylsulfatase Bm showed a similar susceptibility to E. coli phosphatase treatment. Inorganic phosphate and serine phosphate but not mannose 6-phosphate could inhibit this dephosphorylation. There were differences in the susceptibilities to alkaline phosphatase treatment of the arylsulfatase Bm from infant and adult human brain. Endogenous phosphatase also seemed to have a role on the phosphorylated state of arylsulfatase Bm.

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