Evaluation of the amount of acyl-CoA elongases in leek ( Allium porrum L) leaves

• Published in: Biochimica et biophysica acta Vol. 1117; no. 1; pp. 78 - 82
• Main Authors: Bessoule, J.-J., Creach, A., Lessire, R., Cassagne, C.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 21.07.1992; Elsevier
• Subjects: Acyl-Carrier Protein S-Malonyltransferase; Acyl-CoA; acyltransferases; Acyltransferases - analysis; Acyltransferases - immunology; Allium porrum; Allium prrum; Analytical, structural and metabolic biochemistry; antibodies; Antibodies, Monoclonal; Antibody; Biological and medical sciences; Elongating system; enzyme activity; Enzyme-Linked Immunosorbent Assay; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Icosanoyl-CoA synthase; leaves; Microsomes - enzymology; Plants, Edible - enzymology; Precipitin Tests; purification; quantitative analysis; Transferases; Very long chain fatty acid (VLCFA); PBS; Antibody; DTT; Very long chain fatty acid (VLCFA); Allium prrum; Hepes; IgG; Acyl-CoA; Elongating system; DEAE-Cellulose; TCA; Icosanoyl-CoA synthase; VLCFA; ELISA; Liliaceae; Monocotyledones; Enzymatic activity; Angiospermae; Allium porrum; Spermatophyta; Microsome
• ISSN: 0304-4165; 0006-3002; 1872-8006; 1878-2434
• DOI: 10.1016/0304-4165(92)90165-Q

Polyclonial antibodies have been raised against the acyl-CoA elongase purified from leck epidermal cells. The antibodies recognize the fraction containing the elongating activity after DEAE or Ultrogel chromatography and their response with the other fractions is very low. The immune complex is immunoprecipitable with Protein A-Sepharose. 1% of the solubilized proteins from leek epidermis microsomes are immunoprecipitated. The immunoprecipitate contains an elongating activity which is 86 ± 20-times that of the unbound fraction.