Thompson R B, Patchan M W
Department of Biological Chemistry, University of Maryland School of Medicine, Baltimore 21201, USA.
Anal Biochem. 1995 May 1;227(1):123-8. doi: 10.1006/abio.1995.1260.
A new type of fluorescence transduction method for determining zinc in solution is described. The approach is based upon energy transfer from a fluorescent label on an enzyme, human carbonic anhydrase II, to a colored inhibitor which binds to zinc in the enzyme active site. If zinc is present in solution, it binds to the apoenzyme, which in turn permits the inhibitor to bind to the enzyme; the inhibitor is thus in close proximity to the label on the enzyme and thereby quenches the label's fluorescence by Forster energy transfer with a concomitant reduction of its lifetime, which is quantitated by phase fluorometry.
描述了一种用于测定溶液中锌的新型荧光转导方法。该方法基于能量从酶(人碳酸酐酶II)上的荧光标记物转移到与酶活性位点中的锌结合的有色抑制剂。如果溶液中存在锌,它会与脱辅基酶结合,这反过来又使抑制剂能够与酶结合;因此抑制剂与酶上的标记物紧密相邻,从而通过福斯特能量转移淬灭标记物的荧光,并伴随其寿命的缩短,这通过相荧光测定法进行定量。