The human multicatalytic proteinase: affinity purification using a monoclonal antibody

J Biochem Biophys Methods. Feb-Mar 1991;22(2):159-65. doi: 10.1016/0165-022x(91)90028-u.

Abstract

A monoclonal antibody, coupled to Sepharose CL-4B, was used for the rapid purification of the human multicatalytic proteinase in a single chromatographic step under mild conditions. The enzyme was homogeneous as judged by nondenaturing polyacrylamide gel electrophoresis. Electrophoresis under dissociating and reducing conditions revealed at least ten components with molecular masses in the range 22-34 kDa. Affinity-purified enzyme was identical to conventionally purified enzyme with respect to enzymatic properties, molecular mass and subunit composition.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal
  • Chromatography, Affinity / methods*
  • Cysteine Endopeptidases / immunology
  • Cysteine Endopeptidases / isolation & purification*
  • Electrophoresis, Polyacrylamide Gel
  • Female
  • Humans
  • Molecular Sequence Data
  • Multienzyme Complexes / immunology
  • Multienzyme Complexes / isolation & purification*
  • Placenta / enzymology
  • Pregnancy
  • Proteasome Endopeptidase Complex

Substances

  • Antibodies, Monoclonal
  • Multienzyme Complexes
  • Cysteine Endopeptidases
  • Proteasome Endopeptidase Complex