Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-16411
Int J Biol Macromol 1997 Jun 01;203:171-8. doi: 10.1016/s0141-8130(97)01157-4.
Show Gene links Show Anatomy links

Conformation of nucleoplasmin and its interaction with DNA-protamine complex as a simple model of fish sperm nuclei.

Iwata K , Hozumi K , Itoh T , Sakairi N , Tokura S , Katagiri C , Nishi N .


???displayArticle.abstract???
Nucleoplasmin was isolated from Xenopus laevis eggs and purified by an improved method using an open column. Its conformation was investigated spectrophotometrically by UV, CD and fluorescence. It was shown that alpha-helix content of nucleoplasmin was 30-40%, and one of the two tryptophan residues in nucleoplasmin located in the hydrophobic surroundings and the other in the relatively hydrophilic surroundings. The isolated nucleoplasmin was found to decondense sperm nuclei of salmon also, suggesting a possibility of the existence of nucleoplasmin-like protein in fish as well. Collapse of the protamine (salmine)-DNA complex as a simple model for fish sperm nuclei by nucleoplasmin was directly observed by measuring OD320 of aqueous protamine-DNA mixtures. This is a molecular level observation for the removal of protamine from DNA-protamine complex.

???displayArticle.pubmedLink??? 9218166
???displayArticle.link??? Int J Biol Macromol


Species referenced: Xenopus laevis
Genes referenced: npm1