Spik G, Haendler B, Delmas O, Mariller C, Chamoux M, Maes P, Tartar A, Montreuil J, Stedman K, Kocher H P
Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France.
J Biol Chem. 1991 Jun 15;266(17):10735-8.
A novel cyclosporin A binding glycoprotein of 21 kDa was isolated from human milk by several steps of cation exchange chromatography. The corresponding gene was cloned from human T cells, expressed in Escherichia coli and the recombinant protein purified. The protein shares 58% amino acid identity with the cytosolic cyclophilin and is initially synthesized with a hydrophobic leader sequence. The cyclophilin-like protein has also peptidyl-prolyl cis/trans-isomerase activity, although less efficient, that is inhibited by cyclosporin A. The existence of a secreted form of cyclophilin-like protein in addition to the previously known cytosolic cyclophilin implies that these proteins act on different in vivo targets.
通过几步阳离子交换色谱法从人乳中分离出一种新型的21 kDa环孢菌素A结合糖蛋白。从人T细胞中克隆出相应基因，在大肠杆菌中表达并纯化重组蛋白。该蛋白与胞质亲环蛋白有58%的氨基酸同一性，最初合成时带有疏水前导序列。尽管效率较低，但该亲环蛋白样蛋白也具有肽基脯氨酰顺/反异构酶活性，且受环孢菌素A抑制。除了先前已知的胞质亲环蛋白外，亲环蛋白样蛋白分泌形式的存在意味着这些蛋白作用于不同的体内靶点。
