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Elsevier, BBA - Gene Structure and Expression, 2(1219), p. 533-535

DOI: 10.1016/0167-4781(94)90082-5

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The Leishmania infantum histone H3 possesses an extremely divergent N-terminal domain

Journal article published in 1994 by Manuel Soto ORCID, JoséM M. Requena, Gracia Morales, Carlos Alonso
This paper is available in a repository.
This paper is available in a repository.

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Abstract

The isolation of a Leishmania cDNA clone coding for an antigen identified as the histone H3 is described. The nucleotide sequence of the cDNA predicts that the Leishmania histone H3 contains 129 residues and that it has a molecular mass of 14,620 Da. Comparison of the amino acid sequence with the consensus sequence of the eukaryotic histone H3 shows that the Leishmania protein has a highly conserved globular region and an extremely divergent amino-terminal portion.