一种钙调蛋白结合蛋白的特性，该蛋白在巨噬细胞样细胞系J774的三氟拉嗪抗性变体中缺乏。

Speaker M G, Orlow S J, Sturgill T W, Rosen O M

Proc Natl Acad Sci U S A. 1983 Jan;80(2):329-33. doi: 10.1073/pnas.80.2.329.

A calmodulin-binding protein is present in extracts of the macrophage-like mouse cell line J774 and in extracts of thioglycollate-stimulated mouse peritoneal macrophages; it is deficient in variants of J774 resistant to trifluoperazine and in resident peritoneal macrophages. The calmodulin-binding protein [CaMBP (J7)0.5] was purified from J774 and resolved from endogenous cyclic nucleotide phosphodiesterase and protein kinase activities. The protein has an apparent native Mr of 125,000-150,000 and binds calmodulin in a calcium-dependent manner with a Kd of 20 nM. It inhibits the ability of calmodulin to activate phosphodiesterase. Its sedimentation constant in glycerol gradients containing calmodulin was dependent upon the relative concentrations of calmodulin and the calmodulin-binding protein.

一种钙调蛋白结合蛋白存在于巨噬细胞样小鼠细胞系J774的提取物以及巯基乙酸刺激的小鼠腹腔巨噬细胞的提取物中；在对三氟拉嗪耐药的J774变体和常驻腹腔巨噬细胞中缺乏该蛋白。从J774中纯化出钙调蛋白结合蛋白[CaMBP (J7)0.5]，并将其与内源性环核苷酸磷酸二酯酶和蛋白激酶活性分离。该蛋白的表观天然Mr为125,000 - 150,000，以钙依赖的方式结合钙调蛋白，Kd为20 nM。它抑制钙调蛋白激活磷酸二酯酶的能力。在含有钙调蛋白的甘油梯度中，其沉降常数取决于钙调蛋白和钙调蛋白结合蛋白的相对浓度。