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

被引：0
|
作者：
Francescato, P
Lugaro, G
Gianfranceschi, GL
De Angelis, L
Chillemi, F
机构：
[1] Univ Milan, Dept Organ & Ind Chem, I-20133 Milan, Italy
[2] CNR, Inst Hormone Chem, I-20133 Milan, Italy
[3] Univ Perugia, Inst Cell Biol, I-06100 Perugia, Italy
[4] Univ Milan, Inst Pharmacol Sci, Milan, Italy
来源：
JOURNAL OF PEPTIDE SCIENCE | 1997年 / 3卷 / 01期
关键词：
seminal plasma peptides; phosphopeptides; synthesis of peptides; protein kinase NII; DNA-binding peptide;
D O I：
10.1002/(SICI)1099-1387(199701)3:1<54::AID-PSC68>3.0.CO;2-9
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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 DMA transcription. These findings support the hypothesis that phosphorylated acidic domains of nuclear non-histone proteins could bind to DNA, thereby controlling transcription.
引用
收藏
页码：54 / 64
页数：11
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