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J Pept Sci. 1997 Jan-Feb;3(1):54-64.

Purification, sequence determination and synthesis of seminal plasma peptides and synthesis of some of their analogues.

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Department of Organic and Industrial Chemistry, University of Milan, Italy.


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.

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