Literature DB >> 7061451

A high molecular weight nuclear basic protein from the bivalve mollusc Spisula solidissima.

J Ausió, J A Subirana.   

Abstract

A basic protein has been isolated from sperm of the bivalve Spisula solidissima. Its characteristics are reminiscent of both histone H1 and of fish protamines. It is unusual in several respects: it contains similar amounts of lysine (24.8%) and arginine (23.1%), plus a residue of tryptophan per molecule. Its size is very large, approximately 297 amino acid residues. It shows a tendency to aggregate, an unusual property given the strongly charged nature of this protein.

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Year:  1982        PMID: 7061451

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  Presence of a highly specific histone H1-like protein in the chromatin of the sperm of the bivalve mollusks.

Authors:  J Ausio
Journal:  Mol Cell Biochem       Date:  1992-10-07       Impact factor: 3.396

2.  Functional anthology of intrinsic disorder. 1. Biological processes and functions of proteins with long disordered regions.

Authors:  Hongbo Xie; Slobodan Vucetic; Lilia M Iakoucheva; Christopher J Oldfield; A Keith Dunker; Vladimir N Uversky; Zoran Obradovic
Journal:  J Proteome Res       Date:  2007-03-29       Impact factor: 4.466

3.  Coexistence of two chromatin structures in sperm nuclei of the bivalve mollusc Protothaca thaca.

Authors:  C Olivares; M Lila Vera; S Ruíz-Lara
Journal:  Mol Cell Biochem       Date:  1993-08-11       Impact factor: 3.396

Review 4.  The protamine family of sperm nuclear proteins.

Authors:  Rod Balhorn
Journal:  Genome Biol       Date:  2007       Impact factor: 13.583

  4 in total

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