Tightly bound nonprotamine proteins from ram sperm nuclei studied by one- and two-dimensional peptide mapping

Zoya Avramova, Bistra Tasheva

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

The tightly bound proteins of ram sperm nuclei (TBSP) have been recovered as a fraction co-sedimenting with DNA after high salt-urea deprotamination of the nuclei. TBSP were studied by two-dimensional (2D)tryptic peptide mapping and by one-dimensional (1D)-partial proteolysis mapping. The 2D maps revealed a strong homology among the proteins, irrespective of substantial differences in their molecular masses. This homology was supported also by the 1D-mapping data. The 2D-tryptic maps of TBSP were compared to those of lamb liver lamins but no apparent similarity was detected. TBSP were found to react positively to a test for the presence of carbohydrate residues, suggesting that these proteins are glycoproteins as established earlier for the lamins. The 2D maps of several proteins of seminal plasma origin, used as a control, displayed completely different peptide profiles.

Original languageEnglish (US)
Pages (from-to)67-75
Number of pages9
JournalMolecular and cellular biochemistry
Volume74
Issue number1
DOIs
StatePublished - Mar 1987

Keywords

  • nuclear matrix
  • peptide mapping
  • sperm chromatin
  • tightly bound proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

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