Use of immunoadsorbent column chromatography for improved purification of arylsulfatase B from human placenta.
A simple and rapid procedure involving immunoadsorbent column chromatography has been developed for the isolation of lysosomal arylsulfatase B from human placenta. Using this method, we purified the enzyme over 20,000-fold with better recovery (16%) compared to that achieved by the conventional procedure. The enzyme appeared to be homogeneous and had an apparent molecular weight of 58,000 on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) under nonreducing conditions. The purified enzyme migrated as two bands with apparent molecular weights of 43,000 and 8,000 by reductive SDS-PAGE.
Jin
T
T
Biochemistry Laboratory, Hokkaido University School of Medicine, Sapporo, Japan.
Kobayashi
T
T
Honke
K
K
Gasa
S
S
Makita
A
A
D002803:Chondro-4-Sulfatase / Q000737:chemistry / Q000302:isolation & purification*; D002845:Chromatography / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel; D005069:Evaluation Studies as Topic; D005260:Female; D006801:Humans; D007163:Immunosorbent Techniques; D008970:Molecular Weight; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy
D002803:Chondro-4-Sulfatase