Abstract:
:In vitro pepsin treatment of plasma proteins generates biologically active peptides such as enkephalin-related peptides. These peptides were characterized using chromatographic techniques along with a radioimmunoassay procedure involving the use of Leu-enkephalin and Met-enkephalin antisera. Serum albumin is the only existing source of Met-enkephalin-immunoreactive peptides. One of these peptides consists of nine residues with the sequence NH2-Glu-Lys-Leu-Gly-Glu-Tyr-Gly-Phe-Gln; a second immunoreactive peptide might be the hexapeptide NH2-Gly-Glu-Tyr-Gly-Phe-Gln, which has been already identified in a rat serum albumin hydrolysate. Our results indicate that immunoglobulins constitute the main source of Leu-enkephalin-immunoreactive peptides. Immunoreactive NH2-Tyr-Phe-Leu was isolated from pepsin-treated bovine immunoglobulins. Binding experiments and cyclic nucleotide measurements suggested that this peptide was an enkephalin-related peptide. Similar experiments could be carried out to identify the proteins that contain enkephalin-like peptide sequences with the view to investigating the various biological processes occurring in enzymatically treated proteins.
journal_name
Peptidesjournal_title
Peptidesauthors
Garreau I,Pejoan C,Bressollier P,Verneuil B,Cucumel K,Cupo Adoi
10.1016/0196-9781(94)90142-2subject
Has Abstractpub_date
1994-01-01 00:00:00pages
1195-204issue
7eissn
0196-9781issn
1873-5169pii
0196-9781(94)90142-2journal_volume
15pub_type
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