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Purification, Sequence Determination and Synthesis of Seminal Plasma Peptides and Synthesis of Some of Their Analogues
Author(s) -
Francescato Pierangelo,
Lugaro Giuseppe,
Gianfranceschi Gian Luigi,
de Angelis Leonardo,
Chillemi Francesco
Publication year - 1997
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/(sici)1099-1387(199701)3:1<54::aid-psc68>3.0.co;2-9
Subject(s) - pentapeptide repeat , chemistry , peptide , dna , biochemistry , phosphorylation , histone , peptide sequence , microbiology and biotechnology , biology , gene
Three peptides were isolated from bovine seminal plasma and purified to homogeneity. The amino acid sequences, as determined by FAB mass spectrometry, are the following: p Glu‐Ala‐ Glu‐Ser‐Asn‐OH, p Glu‐Ala‐Glu‐Ser(PO 3 H 2 ‐Asn‐OH and p Glu‐Val‐Gly‐Glu‐Ser‐Glu‐Asn‐OH. These three peptides and some of their analogues were synthesized using liquid‐ and solid‐phase techniques. The pentapeptide p Glu‐Ala‐Glu‐Ser‐Asn‐OH showed a remarkable affinity for kinase NII and a strong inhibiting activity in DNA transcription. These findings support the hypothesis that phosphorylated acidic domains of nuclear non‐histone proteins could bind to DNA, thereby controlling transcription. © 1997 European Peptide Society and John Wiley & Sons, Ltd.