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    J Biol Chem. 1994 Feb 11;269(6):4313-6.

    Assignment of disulfide bonds in corticotropin-releasing factor-binding protein.

    Fischer WH, Behan DP, Park M, Potter E, Lowry PJ, Vale W.

    Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, California 92037.

    We have previously isolated, cloned, and characterized a protein that specifically binds and inactivates the peptide corticotropin-releasing factor. The integrity of the disulfide bonds in the binding protein is essential for this activity as reduction abolishes the protein's ability to bind corticotropin-releasing factor. The disulfide arrangement of the 10 cysteines present in the mature protein was established by analysis of proteolytically cleaved protein and sequence analysis of cystine containing fragments. A pattern is observed where each cysteine is connected to the next one in a sequential manner. Inspection of the genomic DNA encoding for this protein reveals that four of the domains defined by disulfide linkage coincide with four different exons.

    PMID: 8307998 [PubMed - indexed for MEDLINE]

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