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PARTIAL PURIFICATION, PROPERTIES AND GLYCOPROTEIN NATURE OF ARYLSULPHATASE B FROM SHEEP BRAIN
Author(s) -
Balasubramanian K. A.,
Bachhawat B. K.
Publication year - 1976
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1976.tb12272.x
Subject(s) - affinity chromatography , enzyme , concanavalin a , glycoprotein , chromatography , chemistry , biochemistry , dissociation (chemistry) , specific activity , ionic strength , sepharose , organic chemistry , in vitro , aqueous solution
— A simple method has been developed for the partial purification of arylsulphatase B from sheep brain. This includes concanavalin A‐Sepharose affinity chromatography and ionic strength‐dependent binding and dissociation of the enzyme with Dextran Blue; by these methods the enzyme was purified 1344‐fold with 10% recovery. The partially purified enzyme was shown to be a glycoprotein and its kinetic properties were compared with that of purified arylsulphatase A from the same source.