Evidence of cross-reactivity between porcine pancreatic and rapeseed (Brassica napus L.) lipases

Biochem Soc Trans. 2000 Dec;28(6):974-6.

Abstract

A cross-reactivity between animal and plant lipases was determined, using immunological techniques. It was shown by ELISA and dot-blotting that these antibodies react with lipases in the rapeseed crude extract and in the different cellular fractions obtained by differential centrifugation. Pre-incubation of the antiserum with the rapeseed crude extract affects the amount of antibodies binding to the porcine pancreatic lipase. Antibodies were able to precipitate lipase activity from 3-day-old rapeseed crude extract. These epitopes seem to be located in the catalytic site, suggesting that a consensus sequence exists in oleaginous lipases and that it will be universal.

MeSH terms

  • Animals
  • Antigen-Antibody Reactions
  • Brassica / immunology*
  • Cotyledon / enzymology
  • Cross Reactions
  • Enzyme-Linked Immunosorbent Assay
  • Kinetics
  • Lipase / immunology*
  • Pancreas / enzymology*
  • Swine

Substances

  • Lipase