Jones A L, Lloyd D, Harwood J L
Department of Biochemistry, School of Pure and Applied Biology, University of Wales College of Cardiff, U.K.
Biochem J. 1993 Nov 15;296 ( Pt 1)(Pt 1):183-8. doi: 10.1042/bj2960183.
The activity of microsomal delta 12-desaturase in Acanthamoeba castellanii was increased after growing cultures were chilled from the optimal growth temperature (30 degrees C) to 15 degrees C. This increase was detectable in microsomes isolated from organisms subjected to only 10 min chilling. The mechanism of induction was investigated. The increase in activity on chilling was greatly reduced when protein synthesis was blocked before the temperature shift. Thus the major mechanism for the induction of delta 12-desaturase is increased protein synthesis. delta 12-Desaturase activity was higher when assayed at 20 degrees C than when assayed at 30 degrees C, but these changes were not due to the increased solubility of O2 at 20 degrees C. The major substrate of delta 12-desaturase was found to be 1-acyl-2-oleoyl phosphatidylcholine.
将生长中的卡氏棘阿米巴培养物从最佳生长温度(30摄氏度)冷却至15摄氏度后,微粒体Δ12-去饱和酶的活性增加。从仅经过10分钟冷却处理的生物体中分离出的微粒体中即可检测到这种增加。对诱导机制进行了研究。当在温度转变前阻断蛋白质合成时,冷却时活性的增加会大大降低。因此,诱导Δ12-去饱和酶的主要机制是蛋白质合成增加。在20摄氏度下测定时,Δ12-去饱和酶的活性高于在30摄氏度下测定时,但这些变化并非由于20摄氏度下氧气溶解度增加所致。发现Δ12-去饱和酶的主要底物是1-酰基-2-油酰磷脂酰胆碱。