Szökefalvi-Nagy Z, Bagyinka C, Demeter I, Kovács K L, Quynh L H
Central Research Institute for Physics, Hungarian Academy of Sciences, Budapest.
Biol Trace Elem Res. 1990 Jul-Dec;26-27:93-101. doi: 10.1007/BF02992662.
A method is presented to identify and determine the relative amounts of protein-bound metal ions in situ. Proteins or their subunits are separated by SDS-PAGE, the appropriately dried gel sections are directly scanned by a collimated proton beam of 3 MeV energy, and the characteristic X-rays produced are detected. The determination of Fe content of an iron-sulfur protein (HiPiP), as well as the Fe and Ni analysis of the hydrogenase from Thiocapsa reseopersicina, have shown the feasibility of this technique.
本文提出了一种原位鉴定和测定蛋白质结合金属离子相对含量的方法。通过SDS-PAGE分离蛋白质或其亚基，用能量为3 MeV的准直质子束直接扫描适当干燥后的凝胶切片，并检测产生的特征X射线。对铁硫蛋白（HiPiP）中铁含量的测定以及对嗜硫红假单胞菌氢化酶中铁和镍的分析，均表明了该技术的可行性。
