31P核磁共振显示蜡样芽孢杆菌磷脂酶C对鞘磷脂的结合与水解作用。
The binding and hydrolysis of sphingomyelin by phospholipase C (Bacillus cereus) as shown by 31P NMR.
作者信息
Aalmo K M, Krane J, Little C, Storm C B
出版信息
Int J Biochem. 1984;16(8):931-4. doi: 10.1016/0020-711x(84)90154-x.
31P nuclear magnetic resonance studies showed that heavily inactivated phospholipase C (Bacillus cereus) initially caused line broadening in the 31P resonance from sphingomyelin thus indicating enzyme-lipid association. Using larger amounts of enzyme or longer preincubation caused a displacement of the 31P resonance to a position suggesting phosphorylcholine formation. Incubation of the heavily inactivated enzyme with a phosphonolipid caused a displacement of the 31P resonance suggesting hydrolysis.
磷-31核磁共振研究表明，严重失活的磷脂酶C（蜡样芽孢杆菌）最初导致鞘磷脂的磷-31共振峰变宽，从而表明酶与脂质发生了结合。使用大量酶或延长预孵育时间会使磷-31共振峰位移至一个表明磷酸胆碱形成的位置。将严重失活的酶与一种磷脂类似物一起孵育会导致磷-31共振峰位移，表明发生了水解。
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