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Characterisation of the single copy trefoil peptides intestinal trefoil factor and pS2 and their ability to form covalent dimers
Author(s) -
Chinery Rebecca,
Bates Paul A.,
De Amitabha,
Freemont Paul S.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01297-e
Subject(s) - trefoil , covalent bond , chemistry , biochemistry , biology , agronomy , organic chemistry
A bacterial recombinant expression system was established to produce biologically active rat Intestinal Trefoil factor (rITF). Characterisation of purified rITF shows that both monomers and dimers can be observed under reducing and non‐reducing conditions, respectively. Site‐directed mutagenesis studies show that Cys57 is necessary for rITF dimer formation. Samples of human gastrointestinal tissue following biopsy also demonstrated the presence of reducible human pS2 and ITF covalent dimers. Three‐dimensional models for pS2 and ITF support the hypothesis that both pS2 and ITF can exist as disulphide‐linked dimers in vivo and that any proposed function for these peptides must take dimer formation into account.