Binding properties and esterase activity of monoclonal antibodies elicited against sucrose 6-heptylphosphonate

Carbohydr Res. 2001 Sep 7;334(4):295-307. doi: 10.1016/s0008-6215(01)00199-9.

Abstract

Various sugar phosphonates were prepared by a Mitsunobu condensation between phosphonic diacids and properly protected carbohydrates. 6'-O-p-Aminophenylsucrose 6-heptylphosphonate was coupled to Bovine Serum Albumin (BSA) and Keyhole Limpet Hemocyanin (KLH) and the KLH conjugate was used for generation of monoclonal antibodies. Binding properties of these antibodies were screened by competitive enzyme-linked immunosorbent assay (ELISA) using the BSA conjugate. A monoclonal antibody with good binding properties showed a regioselective esterase activity toward 6-octanoylsucrose compared with 6'-octanoylsucrose.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Monoclonal / metabolism*
  • Binding Sites, Antibody*
  • Carbohydrate Sequence
  • Enzyme-Linked Immunosorbent Assay
  • Esterases / metabolism*
  • Molecular Sequence Data
  • Organophosphonates / chemistry
  • Organophosphonates / immunology*
  • Organophosphonates / metabolism
  • Sucrose / analogs & derivatives
  • Sucrose / chemical synthesis
  • Sucrose / chemistry
  • Sucrose / immunology*
  • Sucrose / metabolism

Substances

  • Antibodies, Monoclonal
  • Organophosphonates
  • sucrose 6-heptylphosphonate
  • Sucrose
  • Esterases