Open AccessThe Primary Structure of Histone H2A from the Sperm Cell of the Sea Urchin Parechinus angulosus
Author(s) -
STRICKLAND Walter N.,
STRICKLAND Marie S.,
GROOT Petronella C.,
HOLT Claus
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04779.x
Subject(s) - sea urchin , histone , sperm , microbiology and biotechnology , chemistry , biology , genetics , dna
The 125 residues of the histone H2A from the sperm cells of the sea urchin Parechinus angulosus have been positioned. The N terminus is blocked by an acetyl group. Compared to the bovine histone, the sea urchin protein differs in 14 positions.