Krause E G, Wollenberger A
Acta Biol Med Ger. 1976;35(5):543-52.
A modification of the protein binding assay for cyclic guanosine-3',5'-monophosphate (cyclic GMP) is described that is more sensitive and less subject to interference by cyclic AMP than are previously published protein binding methods. The assay employs a purified binding protein from the fat body of the pupa of the common silkmoth, Bombyx mori. The dissociation constant of the binding protein for cyclic GMP is 4.3 nM. A protein kinase modulator protein isolated from the same species increases the binding affinity and capacity of the cyclic GMP binding protein and can be used to advantage in the assay for cyclic GMP. As little as 0.1 pmoles of cyclic GMP can be detected by this procedure. Changes in the level of cyclic GMP in the frog heart during the cardiac cycle were determined by means of the new assay.
本文描述了一种用于环磷酸鸟苷（cGMP）的蛋白质结合测定法的改进方法，该方法比以前发表的蛋白质结合方法更灵敏，且受环磷酸腺苷（cAMP）干扰的影响更小。该测定法使用了从家蚕蛹的脂肪体中纯化得到的结合蛋白。该结合蛋白对cGMP的解离常数为4.3 nM。从同一物种中分离出的一种蛋白激酶调节蛋白可提高cGMP结合蛋白的结合亲和力和容量，并可在cGMP测定中发挥优势。通过该方法可检测低至0.1皮摩尔的cGMP。利用这种新的测定法测定了蛙心在心动周期中cGMP水平的变化。
