长链饱和脂肪酸可被黄瓜（Cucumis sativus）中的一种纯化酶（相对分子质量240,000）进行α氧化。

Long-chain saturated fatty acids can be alpha-oxidised by a purified enzyme (M(r) 240,000) in cucumber (Cucumis sativus).

作者信息

Borge G I, Slinde E, Nilsson A

机构信息

Norwegian Food Research Institute, As, Norway.

出版信息

Biochim Biophys Acta. 1997 Jan 7;1344(1):47-58. doi: 10.1016/s0005-2760(96)00127-0.

DOI:10.1016/s0005-2760(96)00127-0

PMID:9022754

Abstract

An enzyme (M(r) 240,000) with high fatty acid alpha-oxidation activity has been purified from the fruit of cucumber (Cucumis sativus). The specific alpha-oxidation activity in the purified fraction was 370 nmol/min per mg protein determined as liberation of 14CO2 from [1-14C]palmitic acid. alpha-Oxidation activity was observed both in the 12,000 x g pellet and 150,000 x g pellet by differential fractionation of cucumber homogenate. The enzyme was purified about 220-fold to near homogeneity from a 12,000 x g fraction by solubilisation with Triton X-100R, ammonium sulphate precipitation, hydrophobic interaction and anion-exchange chromatographies and Superose 12 gel filtration. The molecular mass of the native enzyme was 240,000, and the major subunit molecular mass of 40,000 indicated an oligomeric structure.

摘要

已从黄瓜（Cucumis sativus）果实中纯化出一种具有高脂肪酸α-氧化活性的酶（相对分子质量240,000）。纯化组分中的比α-氧化活性为每毫克蛋白质370 nmol/分钟，通过[1-¹⁴C]棕榈酸释放¹⁴CO₂来测定。通过对黄瓜匀浆进行差速分级分离，在12,000×g沉淀和150,000×g沉淀中均观察到α-氧化活性。通过用Triton X-100R溶解、硫酸铵沉淀、疏水相互作用和阴离子交换色谱以及Superose 12凝胶过滤，该酶从12,000×g组分中纯化了约220倍，达到近乎纯的状态。天然酶的分子量为240,000，主要亚基分子量为40,000，表明其为寡聚结构。