Open AccessIsolation and comparison of arylsulfatase A from rat liver and Morris hepatoma 7777
Author(s) -
HESS Grzegorz
Publication year - 1983
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1983.tb07680.x
Subject(s) - isoelectric focusing , chemistry , polyacrylamide gel electrophoresis , arylsulfatase a , chromatography , affinity chromatography , isoelectric point , sepharose , polyacrylamide , biochemistry , enzyme , polymer chemistry
Rat liver and Morris hepatoma 7777 arylsulfatase A were isolated from the soluble lysosomal extract by a procedure involving blue‐Sepharose affinity chromatography, DEAE‐cellulose chromatography, hydrophobic chromatography on phenyl‐Sepharose and preparative polyacrylamide gel electrophoresis. The preparation obtained by this method was apparently homogenous in disc electrophoresis and in immunoelectrophoresis. The comparative studies revealed that the properties of arylsulfatase A from rat liver and Morris hepatoma 7777 are very similar, considering molecular weight of the native monomer and its subunits, the ability to form tetramers, isoelectric point, Michaelis constant and the anomalous kinetics of the reaction. The twofold elevation of arylsulfatase B activity found in Morris hepatoma 7777 suggests that the enzyme may have certain functions in tumor growth.