Effects of the catalytic hydrogenation of microsomal lipids upon four enzyme activities involved in oleic acid desaturation

C. Demandre, L. Vigh, A. M. Justin, A. Jolliot, C. Wolf, P. Mazliak

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Abstract

Catalytical hydrogenation of the unsaturated fatty acyl residues of microsomal lipids was realized for different times. Progress of the reaction was followed by calculating the progressive loss of double-bonds in 100 initial acyl residues (percentage of hydrogenation). The maximum loss observed was 45% after 60 min. The drop in polyunsaturated faty acid content was coupled with an increase in the amount of stearic acid and oleic acid. The order parameter of microsomal lipids, measured by ESR, increased parallely to the reduction of double bonds. Maximum hydrogenation of microsomal lipids strongly (200-250%) stimulated microsomal NADH-ferricyanide reductase activity. NADH-cytochrome c reductase, lysophosphatidylcholine-acyl-transferase and oleoyl-phosphatidylcholine desaturase were inhibited (40%, 100% and 100% respectively). These modifications of enzyme activities are discussed in conjunction with the changes observed in membrane fluidity, following hydrogenation of microsomal lipids.

Original languageEnglish
Pages (from-to)13-21
Number of pages9
JournalPlant Science
Volume44
Issue number1
DOIs
Publication statusPublished - 1986

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Keywords

  • Solanum tuberosum
  • hydrogenation
  • membrane fluidity
  • oleate-desaturase
  • polyunsaturated acids

ASJC Scopus subject areas

  • Genetics
  • Agronomy and Crop Science
  • Plant Science

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