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    J Biol Chem. 1991 Jun 15;266(17):10735-8.

    A novel secreted cyclophilin-like protein (SCYLP).

    Spik G, Haendler B, Delmas O, Mariller C, Chamoux M, Maes P, Tartar A, Montreuil J, Stedman K, Kocher HP, et al.

    Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Flandres-Artois, Villeneuve d'Ascq, France.

    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.

    PMID: 2040592 [PubMed - indexed for MEDLINE]

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