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Inter‐alpha‐trypsin‐inhibitor (ITI): two distinct mRNAs in baboon liver argue for a discrete synthesis of ITI and ITI derivatives
Author(s) -
Bourguig J.,
Vercaigne D.,
Sesboüé R.,
Martin J.P.,
Salier J.P.
Publication year - 1983
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(83)80791-1
Subject(s) - baboon , trypsin , chemistry , translation (biology) , alpha (finance) , microbiology and biotechnology , stereochemistry , biochemistry , messenger rna , biology , enzyme , endocrinology , medicine , gene , construct validity , nursing , patient satisfaction
Human serum inter‐alpha‐trypsin‐inhibitor (ITI) has so far been assumed to be comprised of a single polypeptide chain which can undergo fragmentation, whereby inhibitory ITI derivatives are released into the blood stream. It contrast, the analysis of the baboon liver mRNA translation products showed that ITI is made up of heavy and light chain(s). The latter may be excreted independently and very likely corresponds to the so‐called ITI derivatives.