Purification, Sequence Determination and Synthesis of Seminal Plasma Peptides and Synthesis of Some of Their Analogues

✍ Scribed by Pierangelo Francescato; Giuseppe Lugaro; Gian Luigi Gianfranceschi; Leonardo de Angelis; Francesco Chillemi

• Publisher: John Wiley and Sons
• Year: 1997
• Tongue: English
• Weight: 101 KB
• Volume: 3
• Category: Article
• ISSN: 1075-2617
• DOI: 10.1002/(sici)1099-1387(199701)3:1<54::aid-psc68>3.0.co;2-9

✦ Synopsis

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: pGlu-Ala-Glu-Ser-Asn-OH, pGlu-Ala-Glu-Ser(PO3H2-Asn-OH and pGlu-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 pGlu-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.