花生的脂氧合酶同工酶

Lipoxygenase isozymes of peanut.

作者信息

Sanders T H, Pattee H E, Singleton J A

出版信息

Lipids. 1975 Nov;10(11):681-5. doi: 10.1007/BF02532761.

PMID:580

Abstract

Lipoxygenase was isolated and partially purified from peanut seed by ammonium sulfate precipitation, gel filtration, and ion exchange column chromatography. Three isozymes of lipoxygenase were identified. Two had pH optima of 6.2, and the other an optimum of 8.3. Molecular weight of each isozyme was 7.3 x 10(4), as determined by gel filtration. The alkaline optimum isozyme was not inhibited by NaCN and was inhibited by CaCl2 except at very low concentrations. The acid optimum isozymes were inhibited by NaCN and were stimulated by CaCl2 concentrations up to ca. 0.7 mM.

摘要

通过硫酸铵沉淀、凝胶过滤和离子交换柱色谱法从花生种子中分离并部分纯化了脂氧合酶。鉴定出了三种脂氧合酶同工酶。其中两种的最适pH为6.2，另一种的最适pH为8.3。通过凝胶过滤测定，每种同工酶的分子量为7.3×10⁴。最适pH为碱性的同工酶不受NaCN抑制，除极低浓度外，受CaCl₂抑制。最适pH为酸性的同工酶受NaCN抑制，在CaCl₂浓度高达约0.7 mM时受到刺激。