Monoclonal antibodies to the human multicatalytic proteinase (proteasome)

Hybridoma. 1992 Aug;11(4):507-17. doi: 10.1089/hyb.1992.11.507.

Abstract

Multicatalytic proteinase is an intracellular enzyme composed of at least 12 different subunits. Seven murine hybridoma cell lines secreting antibodies to human multicatalytic proteinase (MCP) were established. The antibodies reacted with 4 different subunits of the oligomeric protein. Three of the antibodies bound to identical or closely spaced epitopes on the largest subunit, as shown by binding competition. Some of the antibodies cross-reacted with MCP from rat or rabbit, but none with lobster MCP. Glycoprotein components could not be detected in human MCP. The monoclonal antibodies and two polyclonal rabbit antibodies did not specifically inhibit the enzymatic activity of human MCP. Electrophoretic analysis of MCP immunoprecipitated from human placenta, liver, kidney, or HeLa cell extracts with antibodies to 3 different subunits suggested that the subunit compositions are very similar or identical.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal*
  • Antibody Specificity
  • Binding, Competitive
  • Cross Reactions
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / immunology*
  • Cysteine Endopeptidases / isolation & purification
  • Epitopes
  • Humans
  • Hybridomas / immunology
  • Mice
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / immunology*
  • Multienzyme Complexes / isolation & purification
  • Proteasome Endopeptidase Complex
  • Protein Conformation
  • Species Specificity

Substances

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