Gia. Borge et al., LONG-CHAIN SATURATED FATTY-ACIDS CAN BE ALPHA-OXIDIZED BY A PURIFIED ENZYME (M(R), 240000) IN CUCUMBER (CUCUMIS-SATIVUS), Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1344(1), 1997, pp. 47-58
An enzyme (M(r) 240000) with high fatty acid alpha-oxidation activity
has been purified from the fruit of cucumber (Cucumis sativus). The sp
ecific alpha-oxidation activity in the purified fraction was 370 nmol/
min per mg protein determined as liberation of (CO2)-C-14 from [1-C-14
]palmitic acid. alpha-Oxidation activity was observed both in the 1200
0 X g pellet and 150 000 X g pellet by differential fractionation of c
ucumber homogenate. The enzyme was purified about 220-fold to near hom
ogeneity from a 12000 X g fraction by solubilisation with Triton X-100
R, ammonium sulphate precipitation, hydrophobic interaction and anion-
exchange chromatographies and Superose 12 gel filtration. The molecula
r mass of the native enzyme was 240 000, and the major subunit molecul
ar mass of 40 000 indicated an oligomeric structure.